1000 Sentences With "hydrophobic" | Random Sentence Generator

At a certain very cold point, hydrophobic materials can no longer be counted on to be hydrophobic.

As for a date when the hydrophobic allusion began to

Guaiacol is somewhat hydrophobic, so it doesn't mix well with water.

It also appears to be highly hydrophobic, meaning it's repelled by water.

They're also polarized to reduce glare and treated with a hydrophobic coating.

The company used 900-fill hydrophobic down but only in limited quantities.

That's where space ping-pong with water droplets and hydrophobic paddles comes in.

Plants are naturally hydrophobic, which means that liquids tend to bounce right off them.

Depending on the chemical composition of the ash, it will be hydrophobic or hydrophilic.

For example, fleece, the hydrophobic washable insulating material that the Chouinards later branded Synchilla.

The down is hydrophobic and the ripstop nylon has also been treated with a water-repellent finish.

These include mirrors intended to shame offenders, and hydrophobic paint that bounces urine back onto their shoes.

Adam was testing out Threadsmith's hydrophobic (meaning scared of water) shirts which promise to be extremely stain resistant.

On one side of the chamber is a super-hydrophobic floor, and on the other, a sponge-like ceiling.

Pros: Warm, lightweight, comfortable, built for spending extended periods of time in the outdoorsCons: High price, no hydrophobic down

They ended up with a short made from stretchy, hydrophobic nylon, meaning it won't get water-logged or weighed down.

Hair is hydrophobic and biosorbent, which means it repels water and can collect heavy metals and other contaminants, like oil.

Additionally, the G433 has a "hydrophobic, stain-resistant fabric finish" that is available in Royal Blue, Fire Red, and Triple Black.

These fall onto the super-hydrophobic floor, join together into bigger droplets, then ping off the surface, taking heat with them.

Sulphur and cooking oils are hydrophobic, which means they repel water, but they have an affinity for hydrocarbons like crude oil.

Next, add reagents—chemicals that bind to the mica grains and make them hydrophobic, meaning they don't want to touch water.

Surface tension keeps the droplet of water together, while the hydrophobic paddles repel the water when it comes into contact. [YouTube]

But the kinds of plastic typically used in plastic containers, like polypropylene, have a lower surface energy and are called hydrophobic.

The three-layer jacket is spun from a waterproof but breathable membrane that's lighter and softer-feeling than other hydrophobic fabrics.

In 2015, officials experimented with hydrophobic paint on walls along the street that would send urine back onto the offender's shoes.

Musk acknowledged that the company had this problem with the front radar, but said that some hydrophobic coating "usually" solves the problem.

Micelles can look like little tadpoles, with a head and a tail, but their head is hydrophilic and their tail is hydrophobic.

Hydrophobic T-Shirts Are Miraculous—Until You Wash ThemA few weeks ago, an Australian startup offered to send me a T-shirt.

If the ash is hydrophobic, it will repel the water and may then run off quickly, washing soil away in the process.

This hydrophobic coating not only helps the umbrella shed rain, but also ensures it will dry out quickly once you're safe inside.

Also, their skin is very slippery, or hydrophobic, and that helps their bodies hydroplane as the feet and tail power them forward.

The proposed technology, described in the journal Applied Physics Letters, was inspired by the super-hydrophobic wings of cicadas, which naturally repel water.

On top of that is a soft jersey cotton fitted sheet, a synthetic down pillow, and a hydrophobic duvet to keep you warm.

Dr Varanasi's work started with what are known as super-hydrophobic water-shedding surfaces, a classic natural example of which is a lotus leaf.

When it's coated with methyltrimethoxysilane it becomes hydrophobic too, which allows its porous nature to soak up oil from water without becoming water-logged.

San Francisco has been battling its public urination problem for years, recently resorting to using hydrophobic paint on some walls frequented by local pee streams.

Some bacteria and viruses have lipid membranes that resemble double-layered micelles with two bands of hydrophobic tails sandwiched between two rings of hydrophilic heads.

I recently treated my car with 303 Touchless Sealant, a hydrophobic silicon-based spray, so I was happy to know it wouldn't be stripped away.

The introduction of hydrophobic (aka water-resistant) down has changed this a bit but there are still plenty of traditional down options on the market.

The bag uses high-quality 850+ fill-power hydrophobic goose down as its insulator, which not only makes it warm but soft and lofty, as well.

It comes with the proprietary coating to make it oleophobic, hydrophobic, it repels dirt, oil … I don't even know what that means but I'll believe you.

His latest surface, though, which is even more hydrophobic than the previous ones, goes back to tinkering not with the pockets' contents, but with the surface's geometry.

In has latest video, he shows how a pair of hydrophobic paddles can be used to guide a droplet of water around inside the International Space Station.

The spray uses a SiO2 (silicon dioxide) base to create a hydrophobic and UV barrier on paint, and it's also safe to use on windows and wheels.

My favorite piece was a white table coated in a hydrophobic substance on which Troemel poured a bottle of green Gatorade and a bottle of yellow Gatorade.

The newly creased graphene was incredibly hydrophobic—water rolled right off it—and it also had a 400 per cent higher electrochemical current density than a flat sheet.

Made with 850-fill hydrophobic goose down insulation surrounded by a water-resistant Pertex shell, the Magma 30º is a sleeping bag built for use on the trail.

It appears I am not the only girlfriend to face this mysterious, hydrophobic behavior: 21 Savage didn't drink water regularly until he dated model and erstwhile Smirnoff spokeslady Amber Rose.

While the heads and tails of an olfactory receptor—the parts that sit inside and outside the cell—love water, its middle section is hydrophobic, like the cell membrane that encases it.

The liquid repellent coats, both, the inside and outside of your electronics in a hydrophobic nano material that protects from humidity, weather, accidental splashes, and even an unintended dip trip into water.

Inside you'll find Anna Amélie's large purses, made of hydrophobic leather in dynamic colors (around 62,000 forints), velvet bodysuits (20163,000 forints) by Anna Daubner and funky women's hats (59,000 forints) from Vecsei.

But that is only one of the many tools at our disposal, from 100 percent clean grid to clean fuel standards, direct incentive programs, hydrophobic elimination, and building infrastructure for clean public transportation.

Aside from reducing ice build up on airplanes, or even the giant sweeping blades of a wind turbine, this research could also benefit waterproof garments, which are a big market for hydrophobic materials.

Showing off a teeny-tiny leopard print one-piece in a belfie one day, an assortment of hydrophobic velvet bikinis the next, and a whole lot of under-boob baring two-pieces in between.

The patent describes two parts of a meshing screen cover, a "hydrophobic portion to resist the entry of liquid" and a "hydrophilic portion to aid in the removal of liquid" in the iPhone's audio chambers.

The companies have offered to divest Evonik's precipitated silica business for dental applications in Europe, Middle East and Africa and Huber Silica's precipitated silica business for defoamer applications and its hydrophobic precipitated silica business in Europe.

Outdoor Gear Lab gave the jacket high marks for its stylish and simple design, but it called out Patagonia for not using hydrophobic down, which can be helpful in keeping the jacket's insulation dry in wet conditions.

The 800-fill down is used as an insulator, but curiously it is not hydrophobic as The North Face relies on its durable water repellent (DWR) coating to help prevent moisture from reaching the interior of the jacket.

What we're watching: Companies are taking a variety of approaches to resolving sensor obstructions: Alchemy's hydrophobic coatings, Mighty AI's object detection and data training, SEEVA's sensor scanner cleaning systems, Vaisala's real-time road conditions data, and WaveSense's ground-penetrating radar.

Made entirely from stainless steel and a durable plastic with a hydrophobic coating, this rack sheds water like a duck's back, meaning that you don't have to worry about your drying rack for clean dishes itself being damp and/or dirty.

Their insulating properties are provided by either hydrophobic down (down that is treated to absorb less water) or a synthetic equivalent, which is integrated into the quilted design to provide a maximum level of warmth across the wearer's core section.

He and the co-founder Bradley Feinstein, a former consultant, have patented a nanotechnology process that bonds hydrophobic polymers with natural fibers on the molecular level to make them water- and stain-repellent, a process that can be licensed by clothing brands.

"When an area has burned, soil become hydrophobic, or water resistant, which causes water to rush over soil instead of soak in," The Rocky Mountain Incident Management Team said in an advisory, noting that crews are in place to perform water rescues.

It uses SiO2 (silicon dioxide) technology to create a hydrophobic and UV barrier on the surface of your car to repel water and dirt, and since it's safe to use on paint, glass, and wheels, you don't have to cover windows while spraying.

Mike Eardley, a senior designer at the company, had previously explained to me over the phone how the company's looking beyond the current athleisure trend and designing for a future where people expect the hydrophobic, sweat-wicking, and cooling technology of workout gear built into all their clothes.

Using two hydrophobic paddles, which repel water like a rain coat, Kelly demonstrated in a video tweeted by the Space Station Thursday how microgravity allows for a droplet of water to become a sphere—or ping pong ball, if you will— which can then be bounced between the paddles.

You won't find an ingredients list of essential oils and organically-sourced butterflies — rather, it's powered by cationic resins that bind to the hair to enhance natural texture, the patented "thickening molecule" that creates body, magnetic texturizers to bring out your wave, and hydrophobic resins that control flyaways and add shine.

To mark the occasion, Hadid brought out her best poolside garb, posting a shot of herself to her Instagram lounging in a bright blue deckchair with her legs slightly crossed wearing the Kylie Jenner-approved trend of a hydrophobic velvet string bikini, paired with some yellow-tinted aviators and a gold body chain.

Other features of noteworthiness are the hydrophobic lens coating, which keeps water from drying and leaving behind calcium deposit stains on the lenses, as well as the grippy rubber nose pads, which aren't all that exciting but easy to appreciate when a lot of other sporty shades might slide down your schnoz at the first sign of perspiration.

There are several reasons why oil and water (and water-based solutions like vinegar) resist mixing: oil is less dense than water creating a propensity for it to float on top of H2O, water molecules naturally knit tightly to each other using strong hydrogen bonds, and the fact that oil tends to be hydrophobic, repelling water instead of attracting it.

For hydrophobic ligands (e.g. PIP2) in complex with a hydrophobic protein (e.g. lipid-gated ion channels) determining the affinity is complicated by non-specific hydrophobic interactions. Non-specific hydrophobic interactions can be overcome when the affinity of the ligand is high.

The hydrophobic residues from each STING protomer form hydrophobic interactions between each other at the interface.

Imprinting of arrays with hydrophilic-in- hydrophobic microwells is made possible using an innovative surface energy replication approach by means of a hydrophobic thiol-ene polymer formulation. In this polymer, hydrophobic-moiety-containing monomers self-assemble at the hydrophobic surface of the imprinting stamp, which results in a hydrophobic replica surface after polymerization. After removing the stamp, microwells with hydrophobic walls and a hydrophilic bottom are obtained. Such fast and inexpensive procedure can be utilised in digital microwell array technology toward diagnostic applications.

Perfluoroalkyl moieties, being lipophobic as well as highly hydrophobic, add a new dimension to the hydrophobic segregation effect.

In biochemistry, the hydrophobic effect can be used to separate mixtures of proteins based on their hydrophobicity. Column chromatography with a hydrophobic stationary phase such as phenyl-sepharose will cause more hydrophobic proteins to travel more slowly, while less hydrophobic ones elute from the column sooner. To achieve better separation, a salt may be added (higher concentrations of salt increase the hydrophobic effect) and its concentration decreased as the separation progresses.

Hydrophobic silica can be used to treat other surfaces to become hydrophobic, this is due to the morphology of the silica particles once they adhere to their host. The silica particles then alter the surface of its host material resulting in a hydrophobic surface. Aggregated fumed silica can be applied to large surfaces to render them hydrophobic. Micro and nanoscale structures, resembling ball and block like forms, are attributed to the hydrophobic characteristics.

Hydrophobic mismatch is the difference between the thicknesses of hydrophobic regions of a transmembrane protein and of the biological membrane it spans.Duque, D.; Li, X. J.; Katsov, K.; Schick, M. J. Chem. Phys. 2002, 116, 10478-10484. In order to avoid unfavorable exposure of hydrophobic surfaces to water, the hydrophobic regions of transmembrane proteins are expected to have approximately the same thickness as the hydrophobic (lipid acyl chain) region of the surrounding lipid bilayer.

Hydrophobic silica is a form of silicon dioxide (commonly known as silica) that has hydrophobic groups chemically bonded to the surface. The hydrophobic groups are normally alkyl or polydimethylsiloxane chains. Hydrophobic silica can be processed in different ways; such as fumed silica, precipitated silica, and aerosol assisted self assembly, all existing in the form of nanoparticles.

Biological molecules are amphiphilic or amphipathic, i.e. are simultaneously hydrophobic and hydrophilic. The phospholipid bilayer contains charged hydrophilic headgroups, which interact with polar water. The layers also contain hydrophobic tails, which meet with the hydrophobic tails of the complementary layer.

Hydrophobic interactions between proteins and the chromatographic matrix can be exploited to purify proteins. In hydrophobic interaction chromatography the matrix material is lightly substituted with hydrophobic groups. These groups can range from methyl, ethyl, propyl, octyl, or phenyl groups. At high salt concentrations, non-polar sidechains on the surface on proteins "interact" with the hydrophobic groups; that is, both types of groups are excluded by the polar solvent (hydrophobic effects are augmented by increased ionic strength).

However, the terms "lipophilic" and "hydrophobic" are not synonymous, as can be seen with silicones and fluorocarbons, which are hydrophobic but not lipophilic.

A schematic of a thermodynamically unstable conformation of a generic polypeptide. Note the lower number of hydrophobic contacts than above. Hydrophobic residues are in green and polar residues are in blue. The hydrophobic-polar protein model is the original lattice protein model.

Most commonly, one of the solvents is water, while the second is hydrophobic, such as 1-octanol. Hence the partition coefficient measures how hydrophilic ("water-loving") or hydrophobic ("water-fearing") a chemical substance is. Partition coefficients are useful in estimating the distribution of drugs within the body. Hydrophobic drugs with high octanol-water partition coefficients are mainly distributed to hydrophobic areas such as lipid bilayers of cells.

The water molecules are fixed in these water cages which drives the hydrophobic collapse, or the inward folding of the hydrophobic groups. The hydrophobic collapse introduces entropy back to the system via the breaking of the water cages which frees the ordered water molecules. The multitude of hydrophobic groups interacting within the core of the globular folded protein contributes a significant amount to protein stability after folding, because of the vastly accumulated van der Waals forces (specifically London Dispersion forces). The hydrophobic effect exists as a driving force in thermodynamics only if there is the presence of an aqueous medium with an amphiphilic molecule containing a large hydrophobic region.

Hydrophobic insecticides and herbicides tend to be more active. Hydrophobic agrochemicals in general have longer half-lives and therefore display increased risk of adverse environmental impact.

Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle.

This forms a continuous, spherical lipid bilayer. Hydrophobic interactions (also known as the hydrophobic effect) are the major driving forces in the formation of lipid bilayers. An increase in interactions between hydrophobic molecules (causing clustering of hydrophobic regions) allows water molecules to bond more freely with each other, increasing the entropy of the system. This complex interaction can include noncovalent interactions such as van der Waals, electrostatic and hydrogen bonds.

The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions.

Thesis When the curdling occurs, the ginger protease cuts open the κ-casein so that the hydrophilic C-terminus and the hydrophobic N-terminus separate. This disrupts the stability of the casein micelle. In the hydrophobic effect, the hydrophobic casein coagulates.Zhang P (1999) Study on Milk Clotting of Ginger juice .

Reversed-phase chromatography (also called RPC, reverse-phase chromatography, or hydrophobic chromatography) includes any chromatographic method that uses a hydrophobic stationary phase. RPC refers to liquid (rather than gas) chromatography.

When a small amount of hydrophilic colloid is added to hydrophobic colloids it may coagulate the latter. This is due to neutralisation of the charge on the hydrophobic colloidal particles. However, the addition of large amount of hydrophilic colloid increases the stability of the hydrophobic colloidal system. This is due to adsorption.

Like other GDGTs, crenarchaeol is a membrane lipid with distinct hydrophobic and hydrophilic regions. The long, nonpolar hydrocarbon chains are hydrophobic while the ether-linked glycerol head groups are polar and hydrophilic. In most organisms, the cell membrane consists of a lipid bilayer in which phospholipids arrange with their hydrophobic, nonpolar hydrocarbon tails facing inwards towards one another and their hydrophilic, polar head groups facing outwards to associate with the polar environments of the cytoplasm or cell exterior. This organization is promoted by the hydrophobic effect, which makes it energetically favorable for hydrophobic molecules to isolate themselves away from aqueous environments.

262x262px Minimizing the number of hydrophobic side-chains exposed to water is an important driving force behind the folding process. The hydrophobic effect is the phenomenon in which the hydrophobic chains of a protein collapse into the core of the protein (away from the hydrophilic environment). In an aqueous environment, the water molecules tend to aggregate around the hydrophobic regions or side chains of the protein, creating water shells of ordered water molecules. An ordering of water molecules around a hydrophobic region increases order in a system and therefore contributes a negative change in entropy (less entropy in the system).

The actual nature of FSL micelles has not been determined. However, based on normal structural function of micelles, it is expected that it will be determined in part by the combination of functional group, spacer and lipid together with temperature, concentration, size and hydrophobicity/hydrophilicity for each FSL Kode construct type. Surface coatings will occur via two theoretical mechanisms, the first being direct hydrophobic interaction of the lipid tail with a hydrophobic surface resulting in a monolayer of FSL at the surface (Fig. 5b). Hydrophobic binding of the FSL will be via its hydrophobic lipid tail interacting directly with the hydrophobic (lipophilic) surface.

Teflon and Silicone are commonly used hydrophobic coatings for coronary guide wires. Hydrophobic coatings have a lower surface energy and reduce friction in the arteries by up to 48%. Hydrophobic coatings do not need to be in contact with fluids to form a slippery texture. Hydrophobic coatings maintain tactile sensation in the artery, giving doctors full control of the wire at all times and reducing the risk of perforation; though, the coatings are more thrombogenic than hydrophilic coatings.

This is entropically favorable since water molecules can move much more freely around hydrophilic amino acids than hydrophobic amino acids. In a hydrophobic environment, the hydrophilic amino acids will concentrate at the core of the protein, while the hydrophobic amino acids will be on the exterior. Since the new interactions between the hydrophilic amino acids are stronger than hydrophobic-hydrophilic interactions, this is enthalpically favorable. Once a polypeptide chain is fully folded, it is called a protein.

It involve hydrophobic gating and resembles conduction by Cys-loop ligand-gated anion channels. Possibly, the tendency of hydrophobic or amphipathic transmembrane helices to self-organize into oligomers creates novel ionic pathways through membranes: hydrophobic nanopores, pathways of low selectivity governed by the chaotropic behavior of individual ionic species under the influence of membrane voltage.

Aerogels by themselves are hydrophilic, and if they absorb moisture they usually suffer a structural change, such as contraction, and deteriorate, but degradation can be prevented by making them hydrophobic, via a chemical treatment. Aerogels with hydrophobic interiors are less susceptible to degradation than aerogels with only an outer hydrophobic layer, even if a crack penetrates the surface.

Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. Hydrophobic is often used interchangeably with lipophilic, "fat- loving". However, the two terms are not synonymous.

The S1 pocket of chymotrypsin- like enzymes is more hydrophobic than in trypsin-like proteases. This results in a specificity for medium to large sized hydrophobic residues, such as tyrosine, phenylalanine and tryptophan.

Minimizing the number of hydrophobic side-chains exposed to water by burying them in the center of a folded protein is a driving force related to solvation. Solvation also affects host–guest complexation. Many host molecules have a hydrophobic pore that readily encapsulates a hydrophobic guest. These interactions can be used in applications such as drug delivery, such that a hydrophobic drug molecule can be delivered in a biological system without needing to covalently modify the drug in order to solubilize it.

Many papers have since presented fabrication methods for producing superhydrophobic surfaces including particle deposition, sol-gel techniques, plasma treatments, vapor deposition, and casting techniques. Current opportunity for research impact lies mainly in fundamental research and practical manufacturing. Debates have recently emerged concerning the applicability of the Wenzel and Cassie–Baxter models. In an experiment designed to challenge the surface energy perspective of the Wenzel and Cassie–Baxter model and promote a contact line perspective, water drops were placed on a smooth hydrophobic spot in a rough hydrophobic field, a rough hydrophobic spot in a smooth hydrophobic field, and a hydrophilic spot in a hydrophobic field.

57, e3373, (2011). For these reasons, the hydrophobic interior of the 2D nanosheets could be an attractive platform for loading or embedding hydrophobic cargo, such as drug molecules, fluorophores, aromatic compounds, and metal nanoparticles.

Characteristic of soaps, sodium stearate has both hydrophilic and hydrophobic parts, the carboxylate and the long hydrocarbon chain, respectively. These two chemically different components induce the formation of micelles, which present the hydrophilic heads outwards and their hydrophobic (hydrocarbon) tails inwards, providing a lipophilic environment for hydrophobic compounds. The tail part dissolves the grease (or) dirt and forms the micelle. It is also used in the pharmaceutical industry as a surfactant to aid the solubility of hydrophobic compounds in the production of various mouth foams.

A droplet of water forms a spherical shape, minimizing contact with the hydrophobic leaf. The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules. The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes hydrogen bonding between molecules of water and minimizes the area of contact between water and nonpolar molecules. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute.

Amongst the many benefits of using hydrophobic concrete, it reduces installation time and lowers costs. Use of hydrophobic concrete can reduce the labor time of industrial project because normal concrete involves a corrosion proofing period as well as a waterproofing period. With hydrophobic concrete, both corrosion proofing and waterproofing are done at the same time. Likewise, time reduction reduces installation costs.

Although the acidic patches are not conserved in bacteria, the hydrophobic patch is always present. These hydrophobic and acidic patches are believed to be the recognition/binding sites for the other proteins involved in electron transfer.

Whereas most nuclear receptors have a hydrophobic surface that results in a cleft, NGFI-B has a hydrophilic surface. Cofactors interact with NGFI-B at a hydrophobic region between helices 11 and 12 to modulate transcription.

Debates have recently emerged concerning the applicability of the Wenzel and Cassie-Baxter models. In an experiment designed to challenge the surface energy perspective of the Wenzel and Cassie-Baxter model and promote a contact line perspective, water drops were placed on a smooth hydrophobic spot in a rough hydrophobic field, a rough hydrophobic spot in a smooth hydrophobic field, and a hydrophilic spot in a hydrophobic field. Experiments showed that the surface chemistry and geometry at the contact line affected the contact angle and contact angle hysteresis, but the surface area inside the contact line had no effect. An argument that increased jaggedness in the contact line enhances droplet mobility has also been proposed.

This crucially sets the substrate up for the series of reactions that form the rings. Oxidosqualene is located in the cell’s microsome membranes where it can easily harvest its hydrophobic substrate and turn out its hydrophobic product.

A strong hydrophobic and lipophobic character was observed for all tested compositions.

Most of research on nanocarriers is being applied to their potential use in drug delivery, especially in chemotherapy. Since nanocarriers can be used to specifically target the small pores, lower pH's, and higher temperatures of tumors, they have the potential to lower the toxicity of many chemotherapy drugs. Also, since almost 75% of anticancer drugs are hydrophobic, and therefore demonstrate difficulty in delivery inside human cells, the use of micelles to stabilize, and effectively mask the hydrophobic nature of hydrophobic drugs provides new possibilities for hydrophobic anticancer drugs.

Due to the amino acid sequence and the periodicity of the helices, the leucine side chains are arranged along one face of the α helix and form a hydrophobic surface that modulates dimerization. Hydrophobic residues additional to leucine also form the characteristic 3-4 repeat of α helices involved in “coiled-coil” interactions, and help contribute to the hydrophobic packing that drives dimerization. Together, this hydrophobic surface holds the two subunits together. The basic region of the bZIP domain is just upstream to the leucine zipper, and contains positively charged residues.

Hydrophobic coagulation occurs when a positively charged solution is added with a sodium alkyl sulfate. The coagulation value is smaller when the alkyl chain length of the coagulator is longer. Hydrophobic coagulation occurs when a negatively charged solution contains a cationic surfactant. The coulomb attraction between the head groups and surface competes with the hydrophobic attraction for the entire tail in a favorable manner.

Magic sand or hydrophobic sand is a toy made from sand coated with a hydrophobic compound. The presence of this hydrophobic compound causes the grains of sand to adhere to one another and form cylinders (to minimize surface area) when exposed to water. When the sand is removed from water, it is completely dry and free flowing. Magic sand is also known as Aqua Sand.

The hydrophobic interactions with catalytic loop F583 and DFG motif F595 stabilize the inactive conformation of these structures, decreasing the likelihood of enzyme activation. Further hydrophobic interaction of K483, L514, and T529 with the center phenyl ring increase the affinity of the kinase domain for the inhibitor. Hydrophobic interaction of F595 with the center ring as well decreases the energetic favorability of a DFG conformation switch further.

The following types of liposomes are visible: small monolamellar vesicles, large monolamellar vesicles, multilamellar vesicles, oligolamellar vesicles. A liposome has an aqueous solution core surrounded by a hydrophobic membrane, in the form of a lipid bilayer; hydrophilic solutes dissolved in the core cannot readily pass through the bilayer. Hydrophobic chemicals associate with the bilayer. A liposome can be hence loaded with hydrophobic and/or hydrophilic molecules.

This region contains the most hydrophilic portion of the molecule. A centrally located hydrophobic domain containing a cluster of 172 highly conserved hydrophobic amino acids is thought to be important for translocation of the enzymatic portion of the protein.

Through the addition of diethylaminoethylthiol to the 2-pyrroline group and oxidation of the sulfate of ostreogrycin A, a structurally more hydrophobic compound is formed. This hydrophobic compound contains a readily ionizable group that is available for salt formation.

A well-defined pharmacophore model includes both hydrophobic volumes and hydrogen bond vectors.

Tanford, C., The hydrophobic effect(New York:Wiley.1980).W . Kauzmann, Adv. Protein Chem.

Perfluorocarbons display outstanding chemical and biological inertness, and intense hydrophobic and lipophobic effects.

A schematic of a thermodynamically stable conformation of a generic polypeptide. Note the high number of hydrophobic contacts. amino acid residues are represented as dots along the white line. Hydrophobic residues are in green while polar residues are in blue.

As a result, hydrophobic molecules in the polar mobile phase tend to adsorb to the hydrophobic stationary phase, and hydrophilic molecules in the mobile phase will pass through the column and are eluted first.(Clinical Biochemistry, T.W.Hrubey, 54) Hydrophobic molecules can be eluted from the column by decreasing the polarity of the mobile phase using an organic (non-polar) solvent, which reduces hydrophobic interactions. The more hydrophobic the molecule, the more strongly it will bind to the stationary phase, and the higher the concentration of organic solvent that will be required to elute the molecule. Many of the mathematical and experimental considerations used in other chromatographic methods also apply to RPC (for example, the separation resolution is dependent on the length of the column).

Since the human body contains mostly water, the ability to deliver hydrophobic drugs effectively in humans is a major therapeutic benefit of nanocarriers. Micelles are able to contain either hydrophilic or hydrophobic drugs depending on the orientation of the phospholipid molecules. Some nanocarriers contain nanotube arrays allowing them to contain both hydrophobic and hydrophilic drugs. One potential problem with nanocarriers is unwanted toxicity from the type of nanomaterial being used.

Stores the ink of the ink cartridge. Others contain hydrophobic foam that prevents refilling.

Both Ile and Phe are hydrophobic amino acids and undergo analogous binding to neurophysins.

The hydrophobic mismatch is important for the protein sorting and formation of lipid rafts.

A model based on electron crystallographic density and nuclear magnetic resonance deconvolution has been proposed to explain the binding of docetaxel to β-tubulin. In this T-shaped/butterfly model, a deep hydrophobic cleft exists near the surface of the β-tubulin where three potential hydrogen bonds and multiple hydrophobic contacts bind to docetaxel. The hydrophobic pocket walls contain helices H1, H6, H7 and a loop between H6 and H7 that form hydrophobic interactions with the 3’-benzamido phenyl, 3’-phenyl, and the 2-benzoyl phenyl of docetaxel. 3’-phenyl also has contact with β-sheets B8 and B10.

In another application, multiwall carbon nanotube (MWCNT) and single wall carbon nanotube (SWCNT) tips were used to image amyloid β (1-40) derived protofibrils and fibrils by tapping mode AFM. Functionalized probes can be used in Chemical Force Microscopy (CFM) to measure intermolecular forces and map chemical functionality. Functionalized SWCNT probes can be used for chemically sensitive imaging with high lateral resolution and to study binding energy in chemical and biological system. Probe tips that have been functionalized with either hydrophobic or hydrophilic molecules can be used to measure the adhesive interaction between hydrophobic-hydrophobic, hydrophobic-hydrophilic, and hydrophilic-hydrophilic molecules.

Models like PB and GB allow estimation of the mean electrostatic free energy but do not account for the (mostly) entropic effects arising from solute-imposed constraints on the organization of the water or solvent molecules. This is termed the hydrophobic effect and is a major factor in the folding process of globular proteins with hydrophobic cores. Implicit solvation models may be augmented with a term that accounts for the hydrophobic effect. The most popular way to do this is by taking the solvent accessible surface area (SASA) as a proxy of the extent of the hydrophobic effect.

These ligands allow the quantum dot to bind to various antigens and can be used to specifically target certain cells. This is the driving mechanism for tumor targeting. Core-shell CdSe-ZnS quantum dots can be protected through bioconjugation, using a coordinating ligand and an amphiphilic polymer. One study used tri-n-octylphosphine oxide (TOPO) as a ligand, and a triblock polymer structure consisting of two hydrophobic segments, and one hydrophilic segment, all with hydrophobic hydrocarbon side chains. The strong hydrophobic interactions between the TOPO and polymer hydrocarbon allow the two layers to “bond” to one another, forming a hydrophobic protection structure.

The alpha helices and beta pleated sheets can be amphipathic in nature, or contain a hydrophilic portion and a hydrophobic portion. This property of secondary structures aids in the tertiary structure of a protein in which the folding occurs so that the hydrophilic sides are facing the aqueous environment surrounding the protein and the hydrophobic sides are facing the hydrophobic core of the protein. Secondary structure hierarchically gives way to tertiary structure formation. Once the protein's tertiary structure is formed and stabilized by the hydrophobic interactions, there may also be covalent bonding in the form of disulfide bridges formed between two cysteine residues.

Scheme of a hydrophilic silicon surface Scheme of a hydrophobic silicon surface Direct bonding is mostly referred to as bonding with silicon. Therefore process techniques are divided in accordance with the chemical structure of the surface in hydrophilic (compare to scheme of a hydrophilic silicon surface) or hydrophobic (compare to scheme of a hydrophobic silicon surface). The surface state of a silicon wafer can be measured by the contact angle a drop of water forms. In the case of a hydrophilic surface the angle is small (< 5 °) based on the excellent wettability whereas a hydrophobic surface shows a contact angle larger than 90 °.

A major portion of RPE65's hydrophobic face, residues 109–126, forms an amphipathic alpha helix that likely contributes to the protein's membrane affinity. Additionally, Cys112 is palmitoylated in native RPE65, further supporting the theory that the hydrophobic face of RPE65 is imbedded in the membrane. The hydrophobic face contains the entrance to the large tunnel that leads to the enzyme's active site. The presence of this channel on the hydrophobic face combined with RPE65's demonstrated ability to absorb substrate direction from the lipid bilayer is consistent with RPE65 being partially embedded in the membrane.

They interact through their hydrophobic parts. The trimeric assemblies are stabilized by multiple hydrogen bonds.

The phospholipid bilayer is formed due to the aggregation of membrane lipids in aqueous solutions. Aggregation is caused by the hydrophobic effect, where hydrophobic ends come into contact with each other and are sequestered away from water. This arrangement maximises hydrogen bonding between hydrophilic heads and water while minimising unfavorable contact between hydrophobic tails and water. The increase in available hydrogen bonding increases the entropy of the system, creating a spontaneous process.

In bulk protein purification, a common first step to isolate proteins is precipitation with ammonium sulfate (NH4)2SO4. This is performed by adding increasing amounts of ammonium sulfate and collecting the different fractions of precipitated protein. Subsequently, ammonium sulfate can be removed using dialysis. During the ammonium sulfate precipitation step, hydrophobic groups present on the proteins are exposed to the atmosphere, attracting other hydrophobic groups; the result is formation of an aggregate of hydrophobic components.

Silicone oils worked well, but caused surface disturbances in many applications like paints and papermaking. In 1963 the first antifoams with hydrophobic particles (hydrophobic silica) in light oil were patented. In the early 1970s, hydrophobic waxes like ethylene bis stearamide dispersed in oils developed. These types of defoamers were very efficient, but the oil crisis of 1973 made these too expensive and resulted in a push for reduction of the oil content.

When phospholipids are exposed to water, they self-assemble into a two-layered sheet with the hydrophobic tails pointing toward the center of the sheet. This arrangement results in two “leaflets” that are each a single molecular layer. The center of this bilayer contains almost no water and excludes molecules like sugars or salts that dissolve in water. The assembly process is driven by interactions between hydrophobic molecules (also called the hydrophobic effect).

Amphitropic proteins associate with lipid bilayers via various hydrophobic anchor structures. Such as amphiphilic α-helixes, exposed nonpolar loops, post-translationally acylated or lipidated amino acid residues, or acyl chains of specifically bound regulatory lipids such as phosphatidylinositol phosphates. Hydrophobic interactions have been shown to be important even for highly cationic peptides and proteins, such as the polybasic domain of the MARCKS protein or histactophilin, when their natural hydrophobic anchors are present.

The stability of the dimer is aided by several interactions at the interface between the DHps of each monomer. These include hydrophobic interactions between conserved hydrophobic residues as well as two hydrogen bonds (Thr-252...Glu-316’ and Arg-263...Asn-307’) and one salt bridge (Lys-270...Glu-303’). Further interactions are mediated via hydrogen bonds to water within a cavity inside the coiled coil and flanked by hydrophobic residues. Single monomer.

The binding interaction between collagen and MDP was studied by saturation transfer difference (STD) NMR spectroscopy. The STD results imply that MDP has a relatively stable interaction with the collagen, because of the hydrophobic interactions between the hydrophobic MDP moieties and the hydrophobic collagen surface.N. Hiraishi, N. Tochio, T. Kigawa, M. Otsuki, and J. Tagami, “Monomer-Collagen Interactions Studied by Saturation Transfer Difference NMR”, J Dent Res 92(3):284-288 (2013).

This results in loose proteins that are suitable as binding proteins. These binding interactions can be hydrophobic interactions as proline-rich proteins tend to have exposed hydrophobic regions. The prolines themselves work as additional binding sites for hydrogen bonds by being strong hydrogen acceptors.

7; 455–477. Specific pockets in the binding site of the HIV protease, often referred to as S1, S1',S2 and S2', recognize hydrophobic amino acids on natural substrates. The potency of inhibitors bearing hydrophobic groups complementing these areas is therefore increased.Blum, A. et al.

Figure 4 shows an example of a compound that fits the agonist pharmacophore perfectly. The nitrogen atom of piperazine fits the positive ionizable feature, the benzofuran part fits the aromatic ring and one hydrophobic, and the trifluoromethane part fits another hydrophobic feature of the pharmacophore.

2002, 41, 66–97.] Lipid rafts have a higher hydrophobic thickness than the rest of the lipid bilayer, which may lead to a preferential separation of transmembrane proteins with a higher hydrophobic thickness into the lipid rafts.Van Meer, G. Science. 2002, 296, 855–856.

One proposed use takes advantage of the hydrophobic trichomes, which do not repel oil. This makes them candidates for mopping up oil spills, as they become saturated with oil in thirty seconds. S. molesta trichomes served as a model for a similarly hydrophobic synthetic polycarbonate.

Detergents, like soaps, work because they are amphiphilic: partly hydrophilic (polar) and partly hydrophobic (non- polar). Their dual nature facilitates the mixture of hydrophobic compounds (like oil and grease) with water. Because air is not hydrophilic, detergents are also foaming agents to varying degrees.

An increase in interactions between hydrophobic molecules (causing clustering of hydrophobic regions) allows water molecules to bond more freely with each other, increasing the entropy of the system. This complex process includes non-covalent interactions such as van der Waals forces, electrostatic and hydrogen bonds.

Vernix is hydrophobic. Vernix is believed to assist in the development of the human intestinal microbiota.

Transmembrane peptides or proteins and surrounding lipids can adapt to the hydrophobic mismatch by different means.

In the case of protein folding, the hydrophobic effect is important to understanding the structure of proteins that have hydrophobic amino acids (such as glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan and methionine) clustered together within the protein. Structures of water-soluble proteins have a hydrophobic core in which side chains are buried from water, which stabilizes the folded state. Charged and polar side chains are situated on the solvent-exposed surface where they interact with surrounding water molecules. Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, although formation of hydrogen bonds within the protein also stabilizes protein structure.

For example, if the hydrophilic region and hydrophobic region are similar, a cylindrical shape lipid bilayer is formed; but when the hydrophilic regions is smaller than the hydrophobic region a cone-shaped lipid bilayer is formed.Gerrit Van Meer. Cellular Lipidomics. The EMBO Journal (2005) 24, 3159–3165, .

Hydrophobic soil – soil that is hydrophyllic – causes water to collect on the soil surface rather than infiltrate into the ground. Wild fires generally cause soils to be hydrophobic temporarily, which increases water repellency, surface runoff and erosion in post-burn sites. Soil dispersion due to sodification causes similar problems. Hydrophobic soils are created when hydrocarbon residue is created after organic material is burnt and soaks into empty pore spaces in the soils, making it impervious to water.

The solubility of proteins in aqueous buffers depends on the distribution of hydrophilic and hydrophobic amino acid residues on the protein's surface. Hydrophobic residues predominantly occur in the globular protein core, but some exist in patches on the surface. Proteins that have high hydrophobic amino acid content on the surface have low solubility in an aqueous solvent. Charged and polar surface residues interact with ionic groups in the solvent and increase the solubility of a protein.

During fusion, the hydrophobic tails of a small patch of lipids on the cell membrane are exposed to the aqueous phase surrounding them. This results in very strong hydrophobic attractions (which dominate the repulsive force) between the exposed groups leading to membrane fusion. The attractive van der Waals forces play a negligible role in membrane fusion. Thus, fusion is a result of the hydrophobic attractions between internal hydrocarbon chain groups that are exposed to the normally inaccessible aqueous environment.

3-D structures of a number of cytochrome b5 and yeast flavocytochrome b2 are known. The fold belongs to the α+β class, with two hydrophobic cores on each side of a β-sheet. The larger hydrophobic core constitutes the heme-binding pocket, closed off on each side by a pair of helices connected by a turn. The smaller hydrophobic core may have only a structural role and is formed by spatially close N-terminal and C-terminal segments.

To maintain a hydrophobic surface, the head groups bind closely to the surface, while the hydrophobic micelles stretch far away from the surface. By varying the amount of SAM you coat on a substrate, one could vary the degree of hydrophobicity. Particular superhydrophobic SAMs have a hydrophobic head group binding to the substrate. In one such work, 1-dodecanethiol (DT; CH3(CH2)11SH) is assembled on a Pt/ZnO/SiO2 composite substrate, producing contact angles of 170.3°.

This revealed a hydrophobic pocket around the phenyl ring adjacent to the piperazinylmethyl group of imatinib. Attempts to utilize this pocket to increase efficacy led to the addition of various hydrophobic groups including single fluoro, bromo and chloro substituents. Finally a trifluoromethyl group at position 3 was found to give the best results, with approximately 36-fold improvement over imatinib. The addition of a hydrophobic group now needed to be countered to sustain the solubility of the substance.

It has a simple topology consisting of three α-helices that form a well-packed hydrophobic core.

The contact angles obtained for hydrophobic surfaces are directly related to surface roughnesses by the Wenzel equation.

They are also hydrophobic and repel paint, minimizing the risk of excess droplets impairing the paintwork finish.

The zinc ion is thought to stabilize the loops between the second and third β sheet as well as the fourth and fifth β sheet. The domain is further stabilized by a number of hydrophobic interactions between the hydrophobic inner surface of the β sheet which is packed against the second and third α helices. The outer surface of the β sheet also has many conserved hydrophobic and basic residues. These residues are Lys30, Arg34, Lys46, Pro48, Lys56, Ile58, His60 and Phe62.

The polar groups in the polymer strongly bind water molecules and form hydrogen bonds which also cause hydrophobic effects to occur. These hydrophobic effects can be exploited to design physically crosslinked hydrogels that exhibit self healing abilities. The hydrophobic effects combined with the hydrophilic effects within the hydrogel structure can be balanced through dangling side chains that mediates the hydrogen bonding that occurs between two separate hydrogel pieces or across a ruptured hydrogel. An example of a dangling chain self healing hydrogel network.

The four polypeptide chains are bound to each other by salt bridges, hydrogen bonds, and the hydrophobic effect.

This is similar to the hydrophobic effect in lipid bilayer membranes where nonpolar molecules and in the interior.

Because xenon is soluble both in water and in hydrophobic solvents, it can image various soft living tissues.

The primary amino acid sequence of the Walker B site is , in which represents any hydrophobic amino acid.

NDUFB3 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. Hydropathy analysis revealed that this subunit and 4 other subunits have an overall hydrophilic pattern, even though they are found within the hydrophobic protein (HP) fraction of complex I.

Their hydrophobic tendency was equivalent to that of known nonpolar amino acids such as methionine and tyrosine (tyrosine is polar aromatic but also hydrophobic), those of which were much greater than that of known polar amino acids such as serine and threonine. Hydrophobicity scales, which rank amino acids from most hydrophobic to most hydrophilic, consistently place cysteine towards the hydrophobic end of the spectrum, even when they are based on methods that are not influenced by the tendency of cysteines to form disulfide bonds in proteins. Therefore, cysteine is now often grouped among the hydrophobic amino acids, though it is sometimes also classified as slightly polar, or polar. While free cysteine residues do occur in proteins, most are covalently bonded to other cysteine residues to form disulfide bonds, which play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium.

Initially, silica is hydrophilic due to the presence of the silanol (Si-OH) groups on the surface of the particle. These silanol groups can chemically react with various reagents to render the silica hydrophobic. There are many different methods of processing silica to become hydrophobic, mainly by adding hydrocarbon groups.

Because of this arrangement, the interior of the toroids is not hydrophobic, but considerably less hydrophilic than the aqueous environment and thus able to host other hydrophobic molecules. In contrast, the exterior is sufficiently hydrophilic to impart cyclodextrins (or their complexes) water solubility. They are not soluble in typical organic solvents.

It is surrounded by the hydrophobic environment because of its placement in the plasma membrane. Now it is recognized as an important link in hydrophobic interaction with capsaicin. The binding sites Arg 114 and Glu 761 and the TM3 region in TRPV1, together consist of a binding pocket to vanilloids.

These transporters are commonly called multi-drug resistant (MDR) ABC transporters and sometimes referred to as "hydrophobic vacuum cleaners".

The x-ray crystal structure of calnexin revealed a globular lectin domain and a long hydrophobic arm extending out.

Structural motif in proteins: from two to seven alpha helixes entwined. Each one of these helixes is a repeated 7 amino acid sequence (HPPHCPC), where H refers to hydrophobic amino acids. The position of hydrophobic remains (alpha helix exterior) causes their amphipathic behaviour. The bond between different chains, produced in cytoplasm (aqueous region), is extremely tight, as Van der Waals forces appear between the hydrophobic radicals (H), surrounded by the hydrophilic amino acids (amphipathic molecule). This bond is known as the “Knobs into holes packing”.

RP-HPLC requires the use of organic solvents, which is not favored and current trends are moving away from that. Hydrophobic interaction chromatography requires high concentration salt elutions and eluent cleaning to remove the salt. To address the shortcomings of the previous methods, Kobayashi’s group grafted acrylic acid (anionic acrylate under neutral conditions) and tert-butylacrylamide (hydrophobic) monomers onto PNIPAAm, resulting in PNIPAAm-co-AAc-co-tBAAm (IAtB) onto silica beads as a stationary phase medium. The reason for incorporating both ionic and hydrophobic compounds is multifaceted.

The strength of hydrogen bonds depends on their environment; thus, H-bonds enveloped in a hydrophobic core contribute more than H-bonds exposed to the aqueous environment to the stability of the native state. In proteins with globular folds, hydrophobic amino acids tend to be interspersed along the primary sequence, rather than randomly distributed or clustered together. However, proteins that have recently been born de novo, which tend to be intrinsically disordered, show the opposite pattern of hydrophobic amino acid clustering along the primary sequence.

In this reaction the hydrophobic tails of different pseudopilins mesh together leaving their globular hydrophilic heads exposed. These long hydrophobic tails are able to aggregate together like this due to strong hydrophobic interactions and the end result is that the pseudopilus steadily grows. The assembly and disassembly of these pseudopilus subunits is powered by the secretion ATPase GspE. It is thought that this constant extension and retraction of the pseudopilus causes it to act like a piston and push secretory proteins out through the outer membrane secretin.

The driving mechanism for micellization is the transfer of hydrocarbon chains from water into the oil-like interior. This entropic effect is called the hydrophobic effect. Compared to the increase of entropy of the surrounding water molecules, this hydrophobic interaction is relatively small. The water molecules are highly ordered around the hydrocarbon chain.

Esculentin-2CHa is constituted by thirty-seven amino acids. These amino acids have different characteristics; some are aliphatic and hydrophobic like Alanine and Leucine. Others, for example Phenylalanine, are aromatic and hydrophobic; therefore, they repel water. There are also positively charged amino acids (Arginine and Lysine) and a negatively charged one (Aspartic acid).

The reactive groups provide locations for further chemical processing, which allow you to change the surface properties of the nanoparticles. For anti-graffiti coatings, hydrophobic and oleophobic (oil-fearing) ligands are grafted onto the silica nanoparticles. Hydrophobic ligands are non-polar molecules such as hydrocarbon chains. Oleophobic ligands consist of polar molecules.

The trinuclear Mg2+ complex is critical for binding DMAPP and stabilizing the pyrophosphate leaving group while the growing hydrocarbon tail wedges into a deep hydrophobic pocket. Site-directed mutagenesis studies have shown that the ultimate length of the isoprenoid product is determined by bulky residues (often phenyalanine) at the hydrophobic pocket's base.

Figure 1: Inactive conformation of B-Raf kinase (CR3) domain. P-Loop (orange) hydrophobic interactions with activation loop (gray) residues that stabilize the inactive kinase conformation are shown with sticks. F595 (red) blocks the hydrophobic pocket where the ATP adenine binds (yellow). D576 (orange) is shown as part of the catalytic loop (magenta).

1949 volumetric studies showing that the interior of proteins has very few charges and, hence, is likely to be hydrophobic.

In a recent study, this protein was shown to bind male pheromone components, specifically farnesene, a highly strong hydrophobic terpene.

Electrowetting is the modification of the wetting properties of a surface (which is typically hydrophobic) with an applied electric field.

The crystal structures in hydrophobic concrete are compact enough to prevent humidity from moving through the capillaries of the concrete.

Relying on mainly non-polar, hydrophobic interactions, only non-polar or very weakly polar compounds will adsorb to the surface.

The crystal structure of TIPE2 reveals that it contains a large, hydrophobic central cavity that is poised for cofactor binding.

The α1 and α2 domains, shown in green, are both quite hydrophobic and may both be inserted into the membrane.

Talk of the Nation, 15 August 2008. Pure capsaicin is a hydrophobic, colorless, highly pungent, crystalline to waxy solid compound.

Chlorophyll a has a long hydrophobic tail, which anchors the molecule to other hydrophobic proteins in the thylakoid membrane of the chloroplast. Once detached from the porphyrin ring, this long hydrocarbon tail becomes the precursor of two biomarkers, pristane and phytane, which are important in the study of geochemistry and the determination of petroleum sources.

Some computer models have suggested that the generation of complex organisms is an inescapable feature of evolution. Proteins tend to become more hydrophobic over time, and to have their hydrophobic amino acids more interspersed along the primary sequence. Increases in body size over time are sometimes seen in what is known as Cope's rule.

A hydrophobic surface is generated if the native oxide layer is removed by either plasma treatment or by fluoride containing etching solutions, e.g. hydrogen fluoride (HF) or ammonium fluoride (NH4F). This process enhances the formation of Si-F bonds of the exposed silicon atoms. For hydrophobic bonding it is important to avoid re-hydrophilization, e.g.

NDUFB1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

The air bubbles must selectively adhere to the desired minerals to elevate them to the surface of the slurry while wetting the other minerals and leaving them in the aqueous slurry medium. Particles that can be easily wetted by water are called hydrophilic, while particles that are not easily wetted by water are called hydrophobic. Hydrophobic particles have a tendency to form a separate phase in aqueous media. In froth flotation the effectiveness of an air bubble to adhere to a particle is based on how hydrophobic the particle is.

NDUFA1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

NDUFA2 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane.

First gold nanoparticles capped with tetra-n-octylammonium bromide were produced. Then the capping agent was removed followed by the addition of various ratios of hydrophilic disulfide functionalized ethylene oxide and hydrophobic disulfide functionalized oligo(p-phenylenevinylene). They then attempted to prove that phase separation on the particle surface occurred by comparing the contact angles of water on the surface of a monolayer of the Janus particles with nanoparticles made with only the hydrophobic or hydrophobic ligands. Instead the results of this experiment showed that while there was some phase separation, it was not complete.

The reason they aggregate is that the parts of the protein that do not dissolve in proteolysis are hydrophobic β-pleated sheets. They are usually sequestered in the middle of the protein, while parts of the protein that are more soluble are found near the outside. When they are exposed to water, these hydrophobic pieces tend to aggregate with other hydrophobic pieces. This ball of fragments gets stabilized by GAGs (glycosaminoglycans) and SAP (serum amyloid P), a component found in amyloid aggregations that is thought to stabilize them and prevent proteolytic cleavage.

Crystal structure of c-Fos:c-Jun heterodimer and DNA complex (). In the "Leucine zipper" domain (gray), the hydrophobic residues on c-Fos and hydrophobic residues on c-Jun pack together on the interface of the coiled- coil (leucines are colored in blue, and the other hydrophobic residues are colored in yellow). Residues from the "basic region" (purple) directly interact with the DNA (red). Activator protein 1 (AP-1) is a transcription factor that regulates gene expression in response to a variety of stimuli, including cytokines, growth factors, stress, and bacterial and viral infections.

NDUFAB1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

In order for steroid hormones to cross the lipid bilayer of cells, they must overcome energetic barriers that would prevent their entering or exiting the membrane. Gibbs free energy is an important concept here. These hormones, which are all derived from cholesterol, have hydrophilic functional groups at either end and hydrophobic carbon backbones. When steroid hormones are entering membranes free energy barriers exist when the functional groups are entering the hydrophobic interior of membrane, but it is energetically favorable for the hydrophobic core of these hormones to enter lipid bilayers.

As mentioned previously, Pseudomonas aeruginosa has the ability to metabolise a variety of substrates including n-alkanes, hexadecane and oils. Uptake of these hydrophobic substrates is speculated to rely on the production of rhamnolipids. It is thought that rhamnolipids either cause the Pseudomonas aeruginosa cell surface to become hydrophobic, promoting an interaction between the substrate and the cell, or secreted rhamnolipids emulsify the substrate and allow it to be taken up by the Pseudomonas aeruginosa cell. There is evidence that rhamnolipids are highly adsorbent to the Pseudomonas aeruginosa cell surface, causing it to become hydrophobic.

Other delivery mechanisms that have been developed include CellSqueeze and electroporation. CPPs typically have an amino acid composition that either contains a high relative abundance of positively charged amino acids such as lysine or arginine or has sequences that contain an alternating pattern of polar, charged amino acids and non- polar, hydrophobic amino acids. These two types of structures are referred to as polycationic or amphipathic, respectively. A third class of CPPs are the hydrophobic peptides, containing only apolar residues with low net charge or hydrophobic amino acid groups that are crucial for cellular uptake.

NDUFA3 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane.

Most of the α-KTxs have a positively charged lysine residue, which blocks the pore of the Kvα1 channels, and a hydrophobic residue (mostly Phe or Tyr), which seems crucial in blocking the Kvα1 channels. PBTx1, PBTx2, PBTx3 and PBTx10 lack the hydrophobic residue and PBTx1, PBTx2 and PBTx10 also lack the lysine. The missing of these residues may explain their low affinity towards the Kvα1 channels. A PBTx3 mutant containing the hydrophobic residue indeed had an affinity that was up to 100 times higher than the wild-type PBTx3.

Water droplets roll down an inclined hydrophobic surface. Water droplets on an artificial hydrophobic surface (left) Dettre and Johnson discovered in 1964 that the superhydrophobic lotus effect phenomenon was related to rough hydrophobic surfaces, and they developed a theoretical model based on experiments with glass beads coated with paraffin or TFE telomer. The self-cleaning property of superhydrophobic micro-nanostructured surfaces was reported in 1977. Perfluoroalkyl, perfluoropolyether, and RF plasma -formed superhydrophobic materials were developed, used for electrowetting and commercialized for bio-medical applications between 1986 and 1995.

It is only present in some human proteins. It is an hydrophobic region which holds the protein to the cell membrane.

The ELN gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Multiple transcript variants encoding different isoforms have been found for this gene. Elastin's soluble precursor is tropoelastin.

The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. MT- ND5 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

Caputo GA, London E. Cumulative effects of amino acid substitutions and hydrophobic mismatch upon the transmembrane stability and conformation of hydrophobic alpha-helices. Biochemistry. 2003 Mar 25;42(11):3275-85. Proteins that lack tryptophan may be coupled to a fluorophore. With fluorescence excitation at 295 nm, the tryptophan emission spectrum is dominant over the weaker tyrosine and phenylalanine fluorescence.

However, a 2017 publication reported that IGEPAL 630 was ten-fold more potent than Nonidet P-40 in a tubulin polymerisation assay. All IGEPAL CA surfactants are derived from octylphenol. This serves as the hydrophobic part. Different amounts of ethylene oxide are combined with this part to get a balance of hydrophobic/hydrophilic substances (measured by HLB).

Specific binding to CD to the methylated H3K9 is mediated by three hydrophobic side chains called the "hydrophobic box". Other sites on HP1 will interact with the H3 tails from neighbouring histones which will give structure to the flexible N-terminal tail of the histones. Neighbouring H3 histones can affect HP1 binding by post- translationally modifying the tails.

Sorption isotherms for hexane and methanol show that the adsorbent has a mesoporous structure. Presence of methyl groups on the surface provides their hydrophobic properties. PMSPH particles tend to form a continuous network in the suspension to reduce interaction of the hydrophobic groups SiCH3 with water. These particles can be viewed as 2D sheets rather than 3D solids.

Whereas chaotropicity was first applied to studies of ions, it is equally applicable to alcohols, aromatics, ion mixtures and other solutes. Furthermore, hydrophobic substances known to stress cellular systems (including benzene and toluene) can chaotropically disorder macromolecules, and induce a chaotrope-stress response in microbial cells, even though they partition into the hydrophobic domains of macromolecular systems.

The active sites are regulated allosterically and undergo transitions between open, inactive, and closed, active, states. Indole-3-glycerol binding site: See image 1. Indole and serine binding site: See image 1. Hydrophobic channel: The α and β active sites are separated by a 25 angstrom long hydrophobic channel contained within the enzyme allowing for the diffusion of indole.

Sigma receptors are defined by the presence of one amine binding site and three hydrophobic binding sites nearby in the ligand- binding region. Thus, the N(b) atom in the central piperazine ring serves to interact with the amine binding site and the two phenethyl groups serve to fill two out of the three hydrophobic pockets.

There are three ways to construct UCNP-based drug delivery systems. First, UCNPs can transport hydrophobic drugs, like doxorubicin, by encapsulating them on the particle surface, the hydrophobic pocket. The drug can be released by a pH change. Second, mesoporous silica coated UCNPs can be used, where drugs can be stored and released from the porous surface.

Types of Dendrimer. (1.) Encapsulation Interaction (2.) Conjugated Interaction Dendrimers in drug- delivery systems is an example of various host–guest interactions. The interaction between host and guest, the dendrimer and the drug, respectively, can either be hydrophobic or covalent. Hydrophobic interaction between host and guest is considered "encapsulated," while covalent interactions are considered to be conjugated.

Amphiphiles are molecules that have both hydrophobic and hydrophilic domains. Detergents are composed of amphiphiles that allow hydrophobic molecules to be solubilized in water by forming micelles and bilayers (as in soap bubbles). They are also important to cell membranes composed of amphiphilic phospholipids that prevent the internal aqueous environment of a cell from mixing with external water.

14 (1959) 1. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute. A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions.

The proteins are attached via a lipid tail on p21rac that binds to the hydrophobic region of GDI. Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases. The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.

Care must also be taken to choose an appropriate material and surface preparation for the AFM tip, as hydrophobic surfaces can interact strongly with lipids and disrupt the bilayer structure.J. Schneider, W. Barger and G. U. Lee."Nanometer scale surface properties of supported lipid bilayers measured with hydrophobic and hydrophilic atomic force microscope probes." Langmuir. 19.

It is only 50% slower than a vacuum simulation. This model was later augmented with the hydrophobic effect and called Charmm19/SASA.

SOSUI's algorithm was developed in 1996 at Tokyo University. The name means as much as "hydrophobic", an allusion to its molecular "clients".

The use of hydrophobic interactions, with very few charged interactions, allows the protein to have broad specificity for a range of lipids.

For example, a sterically hindered, large, hydrophobic molecule (Dibutylethanol Amine – DBAE) being protonated to become hydrophilic as necessitated by the reaction process.

Unlike traditional persistent organic pollutants, which are lipophilic and stored primarily in fat tissue, PFOS and PFOA are both lipophobic and hydrophobic.

Cerastocytin contains a hydrophobic domain that binds fibrinopeptide A and in the 3-D confirmation looks very similar to the analogous region of alpha-thrombin. Despite these functional and structural similarities, cerastocytin possesses a distinct amino acid sequence Ile98, Val99, Tyr172, Trp215, which forms the hydrophobic pocket when combined with the 90-loop (Phe90 Val99). The peptides that serve this purpose in thrombin (Leu99, Ile174, Trp215) are known as the aryl binding site and appear to be conserved in many different species. However, the variation in this sequence within the hydrophobic pocket of cerastocytin suggests that the precise amino acid composition is not relevant to fibrinogen binding ability of the protease, as long as there is a non-polar region to interact with the hydrophobic part of the substrate.

While residues in positions a and d are generally hydrophobic and form a zigzag pattern of knobs and holes that interlock with a similar pattern on another strand to form a tight- fitting hydrophobic core, residues in positions e and g are charged residues contributing to the electrostatic interaction. In the case of leucine zippers, leucines are predominant at the d position of the heptad repeat. These residues pack against each other every second turn of the alpha-helices, and the hydrophobic region between two helices is completed by residues at the a positions, which are also frequently hydrophobic. They are referred to as coiled coils unless they are proven to be important for protein function. If that is the case, then they are annotated in the “domain” subsection, which would be the bZIP domain.

Oxytocin possesses Ile-3 whereas vasopressin possesses Phe-3. Both Ile and Phe are hydrophobic amino acids and undergo analogous binding to neurophysins.

The conjugation of glutathione on the previously hydrophobic-toxic substrate results in a soluble compound, which is more readily exocytosed by the cell.

The DED binds to the DED of intracellular molecules such as procaspase 8. It is thought that this interaction occurs through hydrophobic interactions.

UQCRC2 is part of the hydrophobic core of the b-c1 complex and is necessary for the stabilization of Ubiquinol Cytochrome c Reductase.

Additionally, they found it was possible to modify the silica after producing the Janus nanoparticles, making it hydrophobic by reacting it with oleylamine.

MD-2 has a β-cup fold structure composed of two anti-parallel β sheets forming a large hydrophobic pocket for ligand binding.

Lipid bilayers occur when hydrophobic tails line up against one another, forming a membrane of hydrophilic heads on both sides facing the water.

Its active site is a hydrophobic pocket that binds peptides containing proline. Cyclosporine can bind this pocket to inhibit the protein’s enzymatic activity.

Hydrophobic structures also tend to remain clear; these are usually rich in fats, e.g. adipocytes, myelin around neuron axons, and Golgi apparatus membranes.

The cloud point can be affected by many structural parameters of the polymer like the hydrophobic content, architecture and even the molar mass.

The rachis elongates after each conidium is produced, resulting in a long zig-zag extension. The conidia are single-celled, haploid, and hydrophobic.

A hydrotrope is a compound that solubilizes hydrophobic compounds in aqueous solutions by means other than micellar solubilization. Typically, hydrotropes consist of a hydrophilic part and a hydrophobic part (similar to surfactants), but the hydrophobic part is generally too small to cause spontaneous self- aggregation. Hydrotropes do not have a critical concentration above which self-aggregation spontaneously starts to occur (as found for micelle- and vesicle-forming surfactants, which have a critical micelle concentration (cmc) and a critical vesicle concentration (cvc)). Instead, some hydrotropes aggregate in a step-wise self-aggregation process, gradually increasing aggregation size.

The N-terminal alpha helix is apolar, containing a central hydrophobic core with hydrophilic residues at either end, and is uncharged. It is similar in structure to a transmembrane signal peptide and implies that it will anchor at the membrane by burying the hydrophobic core within the bilayer. In particular, the bulky and very hydrophobic phenylalanine residue is important for interacting with uncharged lipid bilayers, such as those composed of phosphatidylcholine. The C-terminal alpha helix is amphipathic with one side displaying polar and charged residues, and the other displaying non-polar residues, which drives insertion into the plasma membrane.

NDUFB4 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I and is of the non- catalytic subunits of the complex. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

NDUFB5 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I and is of the non- catalytic subunits of the complex. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

After the autoinhibitory CR1 regulatory domain is released, B-Raf's CR3 kinase domain must change to its ATP-binding active conformer before it can catalyze protein phosphorylation. In the inactive conformation, F595 of the DFG motif blocks the hydrophobic adenine binding pocket while activation loop residues form hydrophobic interactions with the P-loop, stopping ATP from accessing its binding site. When the activation loop is phosphorylated, the negative charge of the phosphate is unstable in the hydrophobic environment of the P-loop. As a result, the activation loop changes conformation, stretching out across the C-lobe of the kinase domain.

LC3 shares structural homology with ubiquitin, and therefore has been termed a ubiquitin-like protein. LC3 has a LDS (LIR docking site)/hydrophobic binding interface in the N terminus which interacts with LIR (LC3 Interacting Region) containing proteins. This domain is rich in hydrophobic amino acids, the mutation of which impairs the ability of LC3 binding with LIR containing proteins, many of which are autophagy cargo adapter proteins. For example, sequestosome (SQSTM1) interacts with Phe 52 and Leu53 aminoacids present in hydrophobic binding interface of LC3 and any mutation of these amino acids prevents LC3 interaction with SQSTM1.

One investigation conducted research on the structure and found that Nurr1 does not contain a ligand-binding cavity but a patch filled with hydrophobic side chains. Non-polar amino acid residues of Nurr1’s co- regulators, SMRT and NCoR, bind to this hydrophobic patch. Analysis of tertiary structure has shown that the binding surface of the ligand-binding domain is located on the grooves of the 11th and 12th alpha helices. This study also found essential structural components of this hydrophobic patch, to be the three amino acids residues, F574, F592, L593; mutation of any these three inhibits LBD activity.

In fact, protein aggregates have been implicated in a wide variety of disease known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state. This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically hydrophobic.

The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. The MT-ND1 product and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

Standard commercial concrete has an average water absorption of 4-10%. In contrast, hydrophobic concrete has an average of 0.3-1%. An overlooked property of hydrophobic concrete is its ability to repel humidity in the air as well. In contrast to liquid water, water molecules in the air moving with a higher kinetic energy and ultimately exist in a gas-like form.

Structural Details of TMEM241 Isoform 1 Alpha helix wheel diagram of TMEM241 isoform 1 showing hydrophobic and hydrophilic region interactions with lipid membrane. TMEM241 is composed of 9 transmembrane domains forming a hydrophobic integral component of the membrane composed primarily of alpha helices. TMEM241 contains a VRG4 (Vandate Resistance Glycosylation) domain with homology to the sugar transporter domain VRG4 from Saccharomyces cerevisiae (yeast).

There are at least two proteins that compose a cyanobacterium's gas vesicle: GvpA, and GvpC. GvpA forms ribs and much of the mass (up to 90%) of the main structure. GvpA is strongly hydrophobic and may be one of the most hydrophobic proteins known. GvpC is hydrophilic and helps to stabilize the structure by periodic inclusions into the GvpA ribs.

These residues are wrapped around the PK11195 ligand forming a stable hydrophobic binding pocket that can be also regarded as the hydrophobic core of the complex. The mammalian TSPO in a complex with diagnostic ligand is monomeric. The loop located in between TM1 and TM2 helices closes the entrance to the space between helices in which are bound with PK11195 molecule.

The biological membrane is made up of lipids with hydrophobic tails and hydrophilic heads. The hydrophobic tails are hydrocarbon tails whose length and saturation is important in characterizing the cell. Lipid rafts occur when lipid species and proteins aggregate in domains in the membrane. These help organize membrane components into localized areas that are involved in specific processes, such as signal transduction.

The chemoattractant secreted from the oocyte is even more potent. It is a hydrophobic non-peptide molecule which, when secreted from the oocyte, is in complex with a carrier proteinArmon, L., Ben-Ami, I., Ron-El, R. and Eisenbach, M. (2014) Human oocyte-derived sperm chemoattractant is a hydrophobic molecule associated with a carrier protein. Fertil. Steril. 102, 885–890.

HIV Gag is then tightly bound to the membrane surface via three interactions: 1) that between the MA HBR and the PI(4,5)P2 inositol phosphate, 2) that between the extruded myristoyl tail of MA and the hydrophobic interior of the plasma membrane, and 3) that between the PI(4,5)P2 arachidonic acid moiety and the hydrophobic channel along the MA surface.

Hot spots are small areas of turf that are dry and often become hydrophobic. They can be first seen when the grass plants in the area begin to wilt. If the hot spot is not taken care of, the turf in that area will eventually die. Once the soil becomes hydrophobic, it is very hard to get water to penetrate.

Residues in hydrophobic pocket are highlighted in yellow. The base of the pocket is formed by the residue in green (a phenylalanine). A 90 degree rotated monomer structure is shown in Inset 1 to highlight the hydrophobic pocket. A top view of the active site is shown in Inset 2 along with the aspartate mediated trinuclear Mg2+ (silver spheres) catalytic center.

The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. The MT-ND2 product and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. The MT-ND3 product and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

The part of the protein that is embedded in the hydrophobic regions of the bilayer are alpha helical and composed of predominantly hydrophobic amino acids. The C terminal end of the protein is in the cytosol while the N terminal region is in the outside of the cell. A membrane that contains this particular protein is able to function in photosynthesis.

The complex has its own unique properties, such as being nonfluorescent and having a unique absorption spectrum. Dye aggregation is often due to hydrophobic effects—the dye molecules stack together to minimize contact with water. Planar aromatic dyes that are matched for association through hydrophobic forces can enhance static quenching. High temperatures and addition of surfactants tend to disrupt ground state complex formation.

In addition, strong hydrophobic phospholipid-peptide interactions have been discovered in both models. In the two peptide models, the folded parts of the carrier molecule correlate to the hydrophobic domain, although the rest of the molecule remains unstructured. 400px Cell-penetrating peptide facilitated translocation is a topic of great debate. Evidence has been presented that translocation could use several different pathways for uptake.

John Tileston Edsall (3 November 1902 – 12 June 2002) was an early protein scientist, who contributed significantly to the understanding of the hydrophobic interaction.

The N-terminal alpha-helix of this domain is hydrophobic and inserts into the membrane like a wedge and helps to drive membrane curvature.

Furthermore, induced electrostatic charge on the highly resistive plastic caused by high-speed manufacturing equipment during plastic production can increase the pickup of pollutants while in the environment. Electrostatic charge of -9 kv has measured in the moving plastic surface which increase the feasibility of adsorbing air borne pollutants. Additionally, low polarity at the surface of the MPs make them more hydrophobic. This hydrophobic nature allows to adsorption of hydrophobic chemicals into surface of MP. Lipid-loving chemicals like POPs (including polychlorinated biphenyls PCBs, polycyclic aromatic hydrocarbons (PAHs) and organochlorine pesticides such as DDT and DDE) have the right characteristics to adsorp and concentrate on the plastics hydrophobic surface forming a micelle shape-like structure More specifically, pregnant women in particular are in danger of causing birth defects to male infants such as anogenital distance, penile width, and testicular descent.

The interaction between the hydrophilic heads and the hydrophobic tails play a part, as well as the concentration of salt within the solution and surfactants.

The gene product has an N-terminal hydrophobic domain that is not present in other UCPs. Two splice variants have been found for this gene.

See Arsenic contamination of groundwater. # Direct contact membrane distillation (DCMD). Applicable to desalination. Heated seawater is passed along the surface of a hydrophobic polymer membrane.

In the dimer the two ABC cassettes contact each other through hydrophobic interactions at the antiparallel beta-sheet of armI by a two-fold axis.

The hydrophobic region has the hexapeptide sequence Val-Gly-His-Ser- Gln-Gly and is at Ser153 in pancreatic lipases but Ser152 in gastric lipases.

The formation of OTMS monolayers is used for converting hydrophilic surfaces to hydrophobic surfaces, e.g. for use in certain areas of nanotechnology and analytical chemistry.

Hydrophobic silica displays water resistant properties because of its nanostructure and chemical properties. When applied to a surface of a material, the nanoparticles adhere to the host material and prevent liquids from permeating the rough texture. The water only comes into contact with the tips of the nanoparticles coating the outside of the material. Due to lack of attraction, the water is repelled from the hydrophobic silica.

Silica particles can become hydrophobic through plasma polymerization. In this process, plasma polymerized 1,7-octadiene (ppOD) (related to the diene hydrocarbons) is used to deposit polymer films onto the silica particles. The ppOD films are deposited through the use of radio frequencies, along with a reactor containing a rotating chamber. Using low specific energy plasma conditions, the ppOD films chemically render the silica particles hydrophobic.

When hydrophobic concrete is made through the use of an admixture, a powder with the hydrophobic chemicals is added during the batching process. In other words, it is added to the concrete mixture itself when the concrete is laid.The usual dosage is two to three percent of the concrete mixture. Because water is a part of the batching process, an additional curing process is not required.

Most of the repairs were necessary due to the damage of water corrosion in urban areas. Because there is little or no water corrosion, hydrophobic concrete is better preserved than regular concrete, which typically looks worn and aged after a few years. From an environmental standpoint, hydrophobic concrete is also beneficial because it is "green". Its ability to be re-crushed makes it easily reusable.

Dactylysin (, peptide hormone inactivating endopeptidase, PHIE) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe-Phe- and -Phe-Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively This endopeptidase in the skin of the amphibian, Xenopus laevis.

Stryer et al., pp. 333–334. This is known as the hydrophobic effect. In an aqueous system, the polar heads of lipids align towards the polar, aqueous environment, while the hydrophobic tails minimize their contact with water and tend to cluster together, forming a vesicle; depending on the concentration of the lipid, this biophysical interaction may result in the formation of micelles, liposomes, or lipid bilayers.

Another device, called DipTest, has also been developed to detect E. coli. It utilizes porous cellulose blotting paper. One end of the paper strip is coated in a hydrophobic material, while the other is coated with a chemoattractant - a substance which attracts cells based on their chemical properties. At the hydrophobic end, customized chemical reagents are imbedded in the paper in a reaction zone.

The hydrophobic core of the phospholipid bilayer is constantly in motion because of rotations around the bonds of lipid tails. Hydrophobic tails of a bilayer bend and lock together. However, because of hydrogen bonding with water, the hydrophilic head groups exhibit less movement as their rotation and mobility are constrained. This results in increasing viscosity of the lipid bilayer closer to the hydrophilic heads.

SEM-image from the PTFE-silver electrode Since about 1970, PTFEs are used to produce an electrode having both hydrophilic and hydrophobic properties while chemically stable and which can be used as binders. This means that, in places with a high proportion of PTFE, no electrolyte can penetrate the pore system and vice versa. In that case the catalyst itself should be non-hydrophobic.

Despite the capability of the cation exchange chromatography in purification process, hydrophobic interaction chromatography is also employed, usually at the second step as a polishing step. By using relatively small bead-sized cation resin, the cation exchange chromatography can identify and separate between isoforms by the apparent charges in the condition, but hydrophobic interaction chromatography is capable of identification and separation of the isoforms by their hydrophobicity.

Furthermore, high net charges promote disorder because of electrostatic repulsion resulting from equally charged residues. Thus disordered sequences cannot sufficiently bury a hydrophobic core to fold into stable globular proteins. In some cases, hydrophobic clusters in disordered sequences provide the clues for identifying the regions that undergo coupled folding and binding (refer to biological roles). Many disordered proteins reveal regions without any regular secondary structure.

No specific amino acid sequence is uniquely recognized by calpains. Amongst protein substrates, tertiary structure elements rather than primary amino acid sequences are likely responsible for directing cleavage to a specific substrate. Amongst peptide and small-molecule substrates, the most consistently reported specificity is for small, hydrophobic amino acids (e.g. leucine, valine and isoleucine) at the P2 position, and large hydrophobic amino acids (e.g.

The negative surface charges on these globulins usually cause them to repel each other. Heating soy milk denatures the proteins and exposes hydrophobic groups normally oriented toward the inside of the globulin structure. Cations from coagulants bind the negatively charged groups. As the net charges of the protein molecules are neutralized, attractive hydrophobic interactions dominate over repulsive electrostatic charges, and protein aggregates are formed.

A helical-wheel plot can be used to show this repeated pattern. Other α helices buried in the protein core or in cellular membranes have a higher and more regular distribution of hydrophobic amino acids, and are highly predictive of such structures. Helices exposed on the surface have a lower proportion of hydrophobic amino acids. Amino acid content can be predictive of an α -helical region.

Typical pharmacophore features include hydrophobic centroids, aromatic rings, hydrogen bond acceptors or donors, cations, and anions. These pharmacophoric points may be located on the ligand itself or may be projected points presumed to be located in the receptor. The features need to match different chemical groups with similar properties, in order to identify novel ligands. Ligand-receptor interactions are typically “polar positive”, “polar negative” or “hydrophobic”.

They are: a metal binding site (M site), core pocket (Q pocket), hydrophobic pocket (H pocket) and lid region (L region). The M site is placed at the bottom of the hydrophobic pocket with several metal atoms. The metal atoms bind to residues that are completely conserved in all PDE family members. The identity of the metal atoms is not known with absolute certainty.

300px The lipocalin family is a large and diverse family of proteins with functions as small hydrophobic molecule transporters. Beta-lactoglobulin is a typical member of the lipocalin family. Beta-lactoglobulin was found to have a role in the transport of hydrophobic ligands such as retinol or fatty acids. Its crystal structure were determined [e.g. Qin, 1998] with different ligands and in ligand-free form as well.

Hydrogen bonds between molecules of liquid water The hydrophobic effect represents the tendency of water to exclude non-polar molecules. The effect originates from the disruption of highly dynamic hydrogen bonds between molecules of liquid water. Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane, cannot accept or donate hydrogen bonds to water.

Interactions between hydrophobic amino-acid residues and the adjacent membranes cause destabilization of the membranes. This allows the phospholipids in the outer layer of each membrane to interact with each other. The outer leaflets of the two membranes form a hemifusion stalk to minimize energetically unfavorable interactions between hydrophobic phospholipid tails and the environment. This stalk expands, allowing the inner leaflets of each membrane to interact.

The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

NDUFB3 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. This protein localizes to the inner membrane of the mitochondrion as a single-pass membrane protein. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

It breaks the protein folding problem into three separate problems: modeling the protein conformation, defining the energetic properties of the amino acids as they interact with one another to find said conformation, and developing an efficient algorithm for the prediction of these conformations. It is done by classifying amino acids in the protein as either hydrophobic or polar and assuming that the protein is being folded in an aqueous environment. The lattice statistical model seeks to recreate protein folding by minimizing the free energy of the contacts between hydrophobic amino acids. Hydrophobic amino acid residues are predicted to group around each other, while hydrophilic residues interact with the surrounding water.

This effect is lessened by switching to the dye ANS; however, this reagent requires UV excitation. The stability curve and its midpoint value (melting temperature, Tm also known as the temperature of hydrophobic exposure, Th) are obtained by gradually increasing the temperature to unfold the protein and measuring the fluorescence at each point. Curves are measured for protein only and protein + ligand, and ΔTm is calculated. The method may not work very well for protein-protein interactions if one of the interaction partners contains large hydrophobic patches as it is difficult to dissect prevention of aggregation, stabilization of a native folds, and steric hindrance of dye access to hydrophobic sites.

Dabigatran chemical structure with binding pockets highlighted S1(red), S2 (green) and S4 (blue) DTIs that fit in the active binding site have to fit in the hydrophobic pocket (S1) that contains aspartic acid residue at the bottom which recognizes the basic side chain. The S2 site has a loop around tryptophan which occludes a hydrophobic pocket that can recognize larger aliphatic residues. The S3 site is flat and the S4 site is hydrophobic, it has tryptophan lined by leucine and isoleucine. Chemical structure of NAPAP Nα-(2-naphthyl-sulphonyl-glycyl)-DL-p- amidinophenylalanyl-piperidine (NAPAP) binds thrombin in the S1, S2 and S4 pockets.

In their model, they relate the energy stored in the undulations of the membrane surface caused by the mismatch to the elastic properties of the lipids and proteins. They do not include microscopic detail of the lipids, but use as input the known thermodynamic properties of the pure lipid system. They also include indirect lipid-protein interactions induced by the mismatch as well as direct lipid- protein van der Waals-like interactions between the hydrophobic parts of the lipid bilayer and the proteins. The excess "hydrophobic effect" associated with the lipid-protein hydrophobic mismatch, and the elastic deformation free energy of the lipid chains near the protein.

The cavity is lined with charged and polar residues that are likely solvated creating an energetically unfavorable environment for hydrophobic substrates and energetically favorable for polar moieties in amphiphilic compounds or sugar groups from LPS. Since the lipid cannot be stable for a long time in the chamber environment, lipid A and other hydrophobic molecules may "flip" into an energetically more favorable position within the outer membrane leaflet. The "flipping" may also be driven by the rigid-body shearing of the TMDs while the hydrophobic tails of the LPS are dragged through the lipid bilayer. Repacking of the helices switches the conformation into an outward-facing state.

HIC media is amphiphilic, with both hydrophobic and hydrophilic regions, allowing for separation of proteins based on their surface hydrophobicity. Target proteins and their product aggregate species tend to have different hydrophobic properties and removing them via HIC further purifies the protein of interest. Additionally, the environment used typically employs less harsh denaturing conditions than other chromatography techniques, thus helping to preserve the protein of interest in its native and functional state. In pure water, the interactions between the resin and the hydrophobic regions of protein would be very weak, but this interaction is enhanced by applying a protein sample to HIC resin in high ionic strength buffer.

Several techniques are known for the patterning of hydrophobic surfaces through the use of moulded polymers and waxes, by physical processing methods such as ion etching and compression of polymer beads, and by chemical methods such as plasma-chemical roughening, which can all result in ultra-hydrophobic coatings.Roach, P., Shirtcliffe, N. J. & Newton, M. I. Soft Matter 4, 224–240, (2008). While these surfaces are effective self-cleaners, they suffer from a number of drawbacks which have so far prevented widespread application. Batch processing a hydrophobic material is a costly and time-consuming technique, and the coatings produced are usually hazy, precluding applications on lenses and windows, and fragile materials.

Surfactin's structure consists of a peptide loop of seven amino acids (L-aspartic acid, L-leucine, glutamic acid, L-leucine, L-valine and two D-leucines), and a hydrophobic fatty acid chain thirteen to fifteen carbons long which allows it to penetrate cellular membranes. Glutamic acid and aspartic acid residues at positions 1 and 5 respectively, constituting a minor polar domain. On the opposite side, valine residue at position 4 extends down facing the fatty acid chain, making up a major hydrophobic domain. Below critical micellar concentrations (CMCs) the fatty acid tail can extend freely into solution, and then participate in hydrophobic interactions within micelles.

ISSN 0028-646X. The Casparian band is involved in the exodermal cell's ability to regulate water flow movement through the membrane as it is the hydrophobic nature of this band that controls the water entry and exit from the root. Exodermal cells have also found to develop another layer of thickened, tertiary hydrophobic substance on the inside of their plasma membrane walls known as the suberin lamellae which form a protective layer on the inside of the cortex of the exodermis. This layer is composed of a protein called suberin and is also hydrophobic meaning it also contributes to the ability of the exodermis to control water input.

The cross-link formation process is mediated by lysyl oxidase. One of the major reasons that elastin can withstand high levels of stress in the body without experiencing any physical deformation is that the underlying tropoelastin contains domains that are highly hydrophobic. These hydrophobic domains, consisting overwhelmingly of alanine, proline, glycine, and valine, tend towards instability and disorderliness, ensuring that the elastin does not lock into any specific confirmation. Thus, ELPs consisting of the Val-Pro-Gly-X-Gly monomeric units, which bear resemblance to the repetitive tropoelastin hydrophobic domains, are highly disordered below their Tt. Even above their Tt in their aggregated state, ELPs are only partially ordered.

165 degree water contact angle on a surface modified using plasma technology system surface chemistry. The contact angle is the red angle plus 90 degrees. Dew drop on a hydrophobic leaf surface Cutting a water droplet using a superhydrophobic knife on superhydrophobic surfaces Water drops on the hydrophobic surface of grass In chemistry, hydrophobicity is the physical property of a molecule that is seemingly repelled from a mass of water (known as a hydrophobe).Aryeh Ben-Na'im Hydrophobic Interaction Plenum Press, New York, (Strictly speaking, there is no repulsive force involved; it is an absence of attraction.) In contrast, hydrophiles are attracted to water.

IUPAC Goldbook hydrocarbyl groups Hydrocarbons are generally colourless and hydrophobic with only weak odours. Because of their diverse molecular structures, it is difficult to generalize further.

Novel, Water- Based Fluorinated Polymers With Excellent Antigraffiti Properties. JCT Research. 2:8, 617–625. Silicon based coatings are hydrophobic, which means the surface repels water.

Some biosurfactants have low critical micelle concentrations (CMCs), a property which increases the apparent solubility of hydrocarbons by sequestering hydrophobic molecules into the centres of micelles.

The interaction between maraviroc and isoleucine (Ile198) is predicted to be mostly hydrophobic in nature and the interaction between maraviroc and tyrosine (Tyr251) is very limited.

The manganese atom in MMT is coordinated with three carbonyl groups as well as to the methylcyclopentadienyl ring. These hydrophobic organic ligands make MMT highly lipophilic.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA8 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal. Related pseudogenes have also been identified on four other chromosomes.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA12 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA10 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA6 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal. Related pseudogenes have also been identified on four other chromosomes.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA9 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled- coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA13 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA11 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy- terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA7 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal. Related pseudogenes have also been identified on four other chromosomes.

The conserved hydrophobic motif at the C-terminal extension of the kinase domain is bound to the N-terminal lobe of the kinase domain, despite being unphosphorylated.

These ligands encapsulate alkali metal cations (typically Na+ and K+), affording large lipophilic cations. These polyethers have a hydrophilic "interiors" containing the ion and a hydrophobic exterior.

They are amphipathic, meaning they have both hydrophilic and hydrophobic properties, which allows them to surround non-polar substances like oil and grease, isolating them from water.

RI is also rich in leucine (21.5%, compared to 9% in typical proteins) and commensurately lower in other hydrophobic residues, esp. valine, isoleucine, methionine, tyrosine, and phenylalanine.

The size of this protein is 14 kDa in humans. Within the N-terminal half of ARF are highly hydrophobic domains that serve as mitochondrial import sequences.

Linderstrøm-Lang contributed to the training of a whole generation of protein scientists, such as Frederic M. Richards, H. A. Scheraga, Christian B. Anfinsen, William F. Harrington, etc. He is also credited with the insight that the free energy of hydrophobic interactions does not depend only on energy (but also entropy), from his realization that mixing water and alcohol (which contains a hydrophobic methyl group) gives off heat.

DPPC is a variant of phosphatidylcholine. Its structure includes both a hydrophilic "head" and hydrophobic "tails", and it is this arrangement that makes it able to reduce the surface tension of the water layer. The choline radical constitutes the polar hydrophilic head; it is oriented towards and extends into the alveolar liquid. The palmitic acid (C16) chains form the nonpolar hydrophobic tails; these are oriented towards the outer side.

Hydrophobic concrete is produced in a variety of ways that fall under two categories; coatings or admixtures. Both allow the crystal structures to form in the presence of water. When creating hydrophobic concrete through a coating process, a coating is sprayed or brushed onto a porous surfaces. In most cases, it is applied to a regular concrete slab that then undergoes a corrosive process to expose more of the concrete's capillaries.

Reversed-phase chromatography (RPC) is any liquid chromatography procedure in which the mobile phase is significantly more polar than the stationary phase. It is so named because in normal-phase liquid chromatography, the mobile phase is significantly less polar than the stationary phase. Hydrophobic molecules in the mobile phase tend to adsorb to the relatively hydrophobic stationary phase. Hydrophilic molecules in the mobile phase will tend to elute first.

The central hydrophobic domain is proposed to be made up of beta-strand structure and to interact with the lipids. It is the only domain whose sequence is conserved. Models show oleosins having a hairpin-like hydrophobic shape that is inserted inside the triacylglyceride (TAG), while the hydrophilic parts are left outside oil bodies.oleosin Oleosins have been found on oil bodies of seeds, tapetum cells, and pollen but not fruits.

This algorithm is used to define domains in the FSSP domain database. Swindells (1995) developed a method, DETECTIVE, for identification of domains in protein structures based on the idea that domains have a hydrophobic interior. Deficiencies were found to occur when hydrophobic cores from different domains continue through the interface region. RigidFinder is a novel method for identification of protein rigid blocks (domains and loops) from two different conformations.

The results are depicted in the simulations and supported by mass density profiles as well. The mass density profiles show the location of the POPC lipids, water, and ethanol relevant to the hydrophobic core of the membrane and the concentration of ethanol. The mass density of ethanol increases as the concentration increases which indicates ethanol is moving towards the hydrophobic core of the membrane. The membrane becomes partially destroyed.

In the GTP-bound form, ARF conformation changes such that the myristate and hydrophobic N-terminal become more exposed and associate with the membrane. The interconversion between GTP and GDP bound states is mediated by ARF GEFs and ARF GAPs. At the membrane, ARF-GTP is hydrolyzed to ARF-GDP by ARF GAPs. Once in the GDP-bound conformation, ARF converts to a less hydrophobic conformation and dissociates from the membrane.

Like other cyclophilins, PPIC forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. PPIC in particular is composed of 212 residues and contains a hydrophobic, ER-targeting sequence at the N-terminal.

Therefore, most biomass fuels, regardless of origin, produce torrefied products with similar properties—with the exception of ash properties, which largely reflect the original fuel ash content and composition. Hydrophobic behavior: :Torrefied biomass has hydrophobic properties, i.e., repels water, and when combined with densification make bulk storage in open air feasible. Elimination of biological activity: :All biological activity is stopped, reducing the risk of fire and stopping biological decomposition like rotting.

The ionic compound improves interactivity with the ionic species, but raises the LCST significantly. The hydrophobic addition counteracts against the raise in LCST and lowers it to a more standard value, but also interacts with the hydrophobic surfaces of biological compounds. This resulted in successful and resolved elution of angiotensin peptides. Additionally, they were able to tune the retention factor for the analytes through isocratic temperature gradient elution.

In addition, the hydrophobic effect—the association of organic compounds in water—is an electrostatic, non-covalent interaction of interest to chemists. The precise physical origin of the hydrophobic effect originates from many complex interactions, but it is believed to be the most important component of biomolecular recognition in water. For example, Xu and Melcher et al. elucidated the structural basis for folic acid recognition by folate acid receptor proteins.

It has been suggested that inteins could prove useful for achieving allotopic expression of certain highly hydrophobic proteins normally encoded by the mitochondrial genome, for example in gene therapy. The hydrophobicity of these proteins is an obstacle to their import into mitochondria. Therefore, the insertion of a non-hydrophobic intein may allow this import to proceed. Excision of the intein after import would then restore the protein to wild- type.

Most lipids have some polar character in addition to being largely nonpolar. Generally, the bulk of their structure is nonpolar or hydrophobic ("water-fearing"), meaning that it does not interact well with polar solvents like water. Another part of their structure is polar or hydrophilic ("water-loving") and will tend to associate with polar solvents like water. This makes them amphiphilic molecules (having both hydrophobic and hydrophilic portions).

The versatility of the system is controlled not only by changing temperature, but also by adding modifying moieties that allow for a choice of enhanced hydrophobic interaction, or by introducing the prospect of electrostatic interaction. These developments have already brought major improvements to the fields of hydrophobic interaction chromatography, size exclusion chromatography, ion exchange chromatography, and affinity chromatography separations, as well as pseudo-solid phase extractions ("pseudo" because of phase transitions).

Mature pilins and pseudopilins have a lollipop shaped structure, made up of a long hydrophobic tail and a globular hydrophilic head domain. Once in the periplasm in their mature state, the pseudopilins will then often be inserted into the outer leaflet of the inner membrane via their hydrophobic tails. The major pseudopilin present in the pseudopilus is GspG. The pseudopilus forms when the individual pseudopilin subunits polymerize together.

Misfolding processes, typically exposing hydrophobic regions of proteins, often are associated with binding to lipid membranes and subsequent aggregation, for example, during neurodegenerative disorders, neuronal stress and apoptosis.

They can form complexes with nucleic acid and small hydrophobic drugs. The lipid container permits transfection past a cell membrane, whilst the protein capsule can bind chemotherapeutic molecules.

Synzymes from organic molecules: Cyclodextrins are cap structures with a hydrophilic exterior but a hydrophobic interior. If pyridoxal is anchored in the interior the cyclodextran shows transaminase activity.

Day M.F. & M. Briggs (1958) The origin and structure of brochosomes. Journal of Ultrastructure Research 2: 239-244. Brochosomes are hydrophobic and help keep the insect cuticle dry.

The attachment of a hydrophobic aliphatic chain as those present in farnesyl or geranylgeranyl groups allows small G-proteins to tether from membranes and carry out effector functions.

The CYP2J2 contains the following domains: • Hydrophobic binding domains • F-G loop (containing non-conservative mutations) primary membrane binding motif The protein also contains an N-terminal anchor.

While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.

Furthermore, both hydrophobicity and icephobicity can lead to quite complex phenomena, such as self-organized criticality-driven complexity as a result of hydrophobic interactions (during wetting of rough/heterogeneous surfaces or during polypeptide chain folding and looping) or ice crystallization (fractal snowflakes). Note that thermodynamically both the hydrophobic interactions and ice formation are driven by the minimization of the surface Gibbs energy, ΔG = ΔH − TΔS, where H, T, and S are the enthalpy, temperature, and entropy, respectively. This is because in the hydrophobic interactions large positive value of TΔS prevails over a small positive value of ΔH making spontaneous hydrophobic interaction energetically profitable. The so-called surface roughening transition governs the direction of ice crystal growth and occurs at the critical temperature, above which the entropic contribution into the Gibbs energy, TΔS, prevails over the enthalpic contribution, ΔH, thus making it more energetically profitable for the ice crystal to be rough rather than smooth.

Although the fold of the globin superfamily is highly evolutionarily conserved, the sequences that form the fold can have as low as 16% sequence identity. While the sequence specificity of the fold is not stringent, the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent-exposed surface must be avoided in order for the structure to remain stable and soluble. The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell anemia.

One of the most popular lattice models, the hydrophobic-polar model (HP model), features just two bead types—hydrophobic (H) and polar (P)—and mimics the hydrophobic effect by specifying a favorable interaction between H beads. For any sequence in any particular structure, an energy can be rapidly calculated from the energy function. For the simple HP model, this is an enumeration of all the contacts between H residues that are adjacent in the structure but not in the chain. Most researchers consider a lattice protein sequence protein-like only if it possesses a single structure with an energetic state lower than in any other structure, although there are exceptions that consider ensembles of possible folded states.

The cyclohexyl group in the aplaviroc structure is predicted to interact with the receptor in a hydrophobic pocket formed by Ile198, Thr195 and Phe109 and is thought to show quite strong hydrophobic interactions. The researchers predict that the butyl group of aplaviroc is buried within the helical bundle through strong hydrophobic interaction with multiple aromatic residues of the CCR5 receptor. Aplaviroc has a unique feature of preserving two of the natural chemokine protein ligands binding to CCR5 and subsequent activation, whereas maraviroc and the other antagonists almost fully block chemokine-CCR5 interactions. This kind of interference is so far considered to be safe, and individuals that naturally lack CCR5 do not show any obvious health problems.

Elution of the hydrophilic molecules adsorbed to the column packing requires the use of more hydrophilic or more polar solvents in the mobile phase to shift the distribution of the particles in the stationary phase towards that of the mobile phase. Reversed-phase chromatography is a technique using alkyl chains covalently bonded to the stationary phase particles in order to create a hydrophobic stationary phase, which has a stronger affinity for hydrophobic or less polar compounds. The use of a hydrophobic stationary phase is essentially the reverse of normal phase chromatography, since the polarity of the mobile and stationary phases have been inverted – hence the term reversed-phase chromatography. Reversed-phase chromatography employs a polar (aqueous) mobile phase.

It has also been shown that production of rhamnolipids promotes uptake of hexadecane by overcoming the inhibitory effect of the hydrophilic interactions caused by LPS. Production of rhamnolipids is observed on hydrophobic substrates but equally high yields are achievable on other carbon sources such as sugars. Furthermore, although mono-rhamnolipids have been shown to interact with the Pseudomonas aeruginosa cell membrane and cause it to become hydrophobic, di-rhamnolipids do not interact well with the cell membrane because the polar head group is too large to penetrate the LPS layer. Therefore, although Rhamnolipids may play a part in interaction of Pseudomonas aeruginosa with hydrophobic carbon sources, they are likely to have additional functions.

Many very hydrophobic materials found in nature rely on Cassie's law and are biphasic on the submicrometer level. The fine hairs on some plants are hydrophobic, designed to exploit the solvent properties of water to attract and remove sunlight-blocking dirt from their photosynthetic surfaces. Inspired by this lotus effect, many functional superhydrophobic surfaces have been developed. Water striders are insects that live on the surface film of water, and their bodies are effectively unwettable due to specialized hairpiles called hydrofuge; many of their body surfaces are covered with these specialized "hairpiles", composed of tiny hairs spaced so closely that there are more than one thousand microhairs per mm, which creates a hydrophobic surface.

The human homologue of yeast Rad23A is one example of a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The solution structure of human Rad23A UBA(2) showed that the domain forms a compact three-helix bundle. Comparison of the structures of UBA(1) and UBA(2) reveals that both form very similar folds and have a conserved large hydrophobic surface patch which may be a common protein-interacting surface present in diverse UBA domains. Evidence that ubiquitin binds to UBA domains leads to the prediction that the hydrophobic surface patch of UBA domains interacts with the hydrophobic surface on the five-stranded beta-sheet of ubiquitin.

The x-ray crystal structure of human CD14 (4GLP.pdb) reveals a monomeric, bent solenoid structure containing a hydrophobic amino-terminal pocket. CD14 was the first described pattern recognition receptor.

By efficient conversion of hydrophobic polymers into hydrophilic polymer nano-dots (Pdots), polymer-water interfacial contact is therefore increased, which results in significantly improved photocatalytic performance of these materials.

Based on the distribution of other amino acid types, there were five high scoring hydrophobic segments. There were also two transmembrane domains located at 82-98aa and 432-449aa.

Occasionally it can also be driven by entropy without energy input, in cases like the formation of the phospholipid bilayer of a cell, where hydrophobic interactions aggregate the molecules.

The hydrophobic or hydrophilic character of a compound or amino acid is sometimes called its hydropathic character, hydropathicity, or even "hydropathy" (which originally meant the therapeutic use of water).

For example, if a protein binds to a hydrophobic region of the channel (and therefore, has a transmembrane region), the molecule in question might be composed of the amino acids alanine, leucine, or phenylalanine, as they are all hydrophobic themselves. Electrophysiology is also an important tool in identifying channel structure, as analyzing the ionic factors that lead to channel activation can be critical to understanding the inhibiting actions of open channel block molecules.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

MBs can facilitate the local targeting of hydrophobic drugs through the incorporation of these agents into the MB lipid shell. This encapsulation technique reduces systemic toxicity, increases drug localization, and improves the solubility of hydrophobic drugs. For increased localization, a targeting ligand can be appended to the exterior of the MB. This improves treatment efficacy. One drawback of the lipid-encapsulated MB as a drug delivery vehicle is its low payload efficacy.

With a hydrophobic interior and hydrophilic exterior, cyclodextrins form complexes with hydrophobic compounds. Alpha-, beta-, and gamma-cyclodextrin are all generally recognized as safe by the U.S. FDA.GRAS Notice No. GRN 000155, alpha-cyclodextrin;GRAS Notice No. GRN 000074, beta- cyclodextrin;GRAS Notice No. GRN 000046, gamma-cyclodextrin They have been applied for delivery of a variety of drugs, including hydrocortisone, prostaglandin, nitroglycerin, itraconazol, chloramphenicol. The cyclodextrin confers solubility and stability to these drugs.

The pharmacophore model of PDE5 usually consists of one hydrogen bond acceptor, one hydrophobic aliphatic carbon chain and two aromatic rings. Small hydrophobic pocket and H-loop of PDE5 enzyme are important for binding affinity of PDE5 inhibitors. As well as positional and conformational changes are observed upon inhibitor binding in many cases. The active site of PDE5 is located at a helical bundle domain at the center of C domain (catalytic domain).

The name differential scanning fluorimetry (DSF) was introduced later but thermofluor is preferable as thermofluor is no longer trademarked and differential scanning fluorimetry is easily confused with differential scanning calorimetry. SYPRO Orange binds nonspecifically to hydrophobic surfaces, and water strongly quenches its fluorescence. When the protein unfolds, the exposed hydrophobic surfaces bind the dye, resulting in an increase in fluorescence by excluding water. Detergent micelles will also bind the dye and increase background noise dramatically.

These Janus nanoparticles were then functionalized by the addition of various ligands with specific affinity for either the iron or silver. This method can also use gold or iron-platinum instead of magnetite. A similar method is the gas–liquid interface method developed by Pradhan et al. In this method, hydrophobic alkane thiolate gold nanoparticles were placed in water, causing the formation of a monolayer of the hydrophobic gold nanoparticles on the surface.

Lipid bilayers are generally impermeable to ions and polar molecules. The arrangement of hydrophilic heads and hydrophobic tails of the lipid bilayer prevent polar solutes (ex. amino acids, nucleic acids, carbohydrates, proteins, and ions) from diffusing across the membrane, but generally allows for the passive diffusion of hydrophobic molecules. This affords the cell the ability to control the movement of these substances via transmembrane protein complexes such as pores, channels and gates.

While these materials have well maintained mechanical strength and structural integrity, they exhibit a hydrophobic nature. This hydrophobicity inhibits their biocompatibility, which makes them less effective for in vivo use as tissue scaffolding. In order to fix the lack of biocompatibility, much research has been done to combine these hydrophobic materials with hydrophilic and more biocompatible hydrogels. While these hydrogels have a superior biocompatibility, they lack the structural integrity of PLA, PCL, and PGA.

Also known as Complex I, this enzyme is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. MT-ND6 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

Hydropathy plot of hexokinase The potential transmembrane portions of a protein can be detected by hydropathy analysis. A hydropathy analysis uses an algorithm that quantifies the hydrophobic character at each position along the polypeptide chain. One of the accepted hydropathy scales is that of Kyte and Doolittle which relies on the generation of hydropathy plots. In these plots, the negative numbers represent hydrophilic regions and the positive numbers represent hydrophobic regions on the y-axis.

The specific activities of sv-LAAOs with various L-amino acids have been explored. Many studies show that a number of sv-LAAOs exhibit a preference for hydrophobic L-amino acids as substrates. For example, results have indicated that most sv-LAAOs demonstrate relatively high specificities toward hydrophobic amino acids such as L-Met, L-Leu, and L-Ile in addition to aromatic amino acids such as L-Phe and L-Trp.

This Valine is important in hydrophobic interaction of Phenylalanine of IGF-1. A substitution to a Glycine at this position is thought to introduce additional flexibility leading to a change of loop conformation, thereby disrupting the hydrophobic interaction that stabilises the complex. At amino acid position 98 the unedited transcript contains a lysine. This residue makes some non specific interactions via the aliphatic part of the side chain with Glu-38 of IGF-1.

Skin based analyte detection is now possible without damaging and continuous replacing of the electrodes as this paper will be immune to sweat. With its endless applications this field of material science is sure to be more explored. A recent application of hydrophobic structures and materials is in the development of micro fuel cell chips. Reactions within the fuel cell produce waste gas CO2 which can be vented out through these hydrophobic membranes.

Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins. When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer.

Alveoli are the spherical outcroppings of the respiratory bronchioles. Pulmonary surfactant is a surface-active lipoprotein complex (phospholipoprotein) formed by type II alveolar cells. The proteins and lipids that make up the surfactant have both hydrophilic and hydrophobic regions. By adsorbing to the air-water interface of alveoli, with hydrophilic head groups in the water and the hydrophobic tails facing towards the air, the main lipid component of surfactant, dipalmitoylphosphatidylcholine (DPPC), reduces surface tension.

Complementing the TPU-trading business, paint protection films were launched in 2020 after five years of development and testing in tropical climates with hydrophobic, self-heating and stain-resistance features.

HIV-2 retropepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase for which the P1 residue is preferably hydrophobic This enzyme belongs to the peptidase family A2.

The defective exports of the mutant MBPs are consistent with the alpha-helical conformation and hydrophobic interactions of the signal peptide in its interaction with the translocon motor protein SecA.

F1 has a water-soluble part that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO F1 creates a pathway for protons movement across the membrane.

Lipid bilayers are structures of lipid molecules consisting of a hydrophobic tail and a hydrophilic head group. Therefore, these structures experience all the characteristic Interbilayer forces involved in that regime.

While native whey protein does not aggregate upon renneting or acidification of milk, denaturing the whey protein triggers hydrophobic interactions with other proteins, and the formation of a protein gel.

Clb5 is 435 amino acids (50.4 kDa). The hydrophobic box motif is found on the C terminus of both cyclins, and includes the conserved FLRRISK sequence characterizing B-type cyclins.

Common to many of them is that the hydrophobic face of the antimicrobial peptide forms pores in the plasma membrane after associating with the fatty chains at the membrane core.

The VASt domain is predominantly associated with lipid binding domains, such as GRAM. It is most likely to function in binding large hydrophobic ligands and may be specific for sterol.

When overexpressed, has been shown to inhibit viral replication. F- Fusion protein. Type I glycoprotein that facilitates fusion between the virus and the host cell membrane. SH- Small hydrophobic protein.

The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal. Related pseudogenes have also been identified on four other chromosomes.

In addition, the transient exposure of a covalently-independent hydrophobic γ-peptide is responsible for breaching cellular membranes and is thus essential for the viral entry of FHV into host cells.

Ara h 3 forms homotrimers and has a highly stable structure, mediated through hydrophobic interactions. It has been established as an allergen. The trimeric assemblies are stabilized by multiple hydrogen bonds.

The human homologue of TMEM205 is 189 amino acids long and has a molecular weight of 21.2 kDa. It contains 4 hydrophobic helical domains that are predicted to be transmembrane domains.

Visual inspection of selective β3-AR agonists revealed that they bind deep in the binding pocket of the receptors and exhibit some H-bonds and or hydrophobic interactions with the receptor.

This also ensures good bioavailability as well as maintaining firm binding strength. The Xa inhibitors currently on market today, therefore rely on hydrophobic and hydrogen bonding instead of highly polar interactions.

Journal of Physical Chemistry B (2008), 112(35), 10841-10847 where the backbone block is hydrophilic and the comb branches are hydrophobic, and dendronized block copolymers,Yi, Zhuo; Liu, Xuanbo; Jiao, Qing; Chen, Erqiang; Chen, Yongming; Xi, Fu. Journal of Polymer Science, Part A: Polymer Chemistry (2008), '46'(12), 4205-4217 where the dendrimer portion is hydrophilic. In the case of diblock, comb and dendronized copolymers the polymersome membrane has the same bilayer morphology of a liposome, with the hydrophobic blocks of the two layers facing each other in the interior of the membrane. In the case of triblock copolymers the membrane is a monolayer that mimics a bilayer, the central block filling the role of the two facing hydrophobic blocks of a bilayer.

The HSP70 chaperone family is the main HSP system within cells, playing a key role in translation, post-translation, prevention of aggregates and refolding of aggregated proteins. When a nascent protein is being translated, HSP70 is able to associate with the hydrophobic regions of the protein to prevent faulty interactions until translation is complete. Post-translational protein folding occurs in a cycle where the protein becomes bound/released from the chaperone allowing burying hydrophobic groups and aiding in overcoming the energy needed to fold in a timely fashion. HSP70 plays a part in de-aggregating proteins using the aforementioned mechanism; the chaperone will bind to exposed hydrophobic residues and either partially or fully disassemble the protein, allowing HSP70 to assist in the proper refolding.

Yak wool has similar properties to other animal fibers, including breathability and static-resistance, but has been proven to outperform sheep wool in a number of areas. Warmth: In woollen garments, air pockets are created between the fibers that reduce the rate of heat transfer. This property combined with lanolin (a hydrophobic grease present in wool fibers) allowing wool to keep you warm when wet. Yak wool is rich in myristic acid, a type of hydrophobic fatty acid.

Semi-permeable foam dressing: This dressing is made up of foam with hydrophilic (attracted to water) properties and outer layer of hydrophobic (repelled from water) properties with adhesive borders. The hydrophobic layer protects the wound from the outside fluid contamination. Meanwhile, the inner hydrophilic layer is able to absorb moderate amount of discharge from the wound. Therefore, this type of dressing is useful for wound with high amount of discharge and for wound with granulation tissue.

A GST monomer binds a glutathione molecule to its N-terminal glutathione-binding site. On the adjacent hydrophobic alpha-helical binding site on the C-terminal domain, the GST binds a hydrophobic xenobiotic molecule. Formation of the active site recruits another GST monomer to interact with the system and the enzymes dimerize. The active GST complex catalyzes the -SH residue on glutathione to perform a nucleophilic attack on electrophilic carbon, sulfur, or nitrogen atoms of the xenobiotic substrate.

Vinyl neodecanoate is mainly used as a modifying monomer in conjunction with other monomers and particularly the manufacture of vinyl acetate based polymer emulsions by the process of emulsion polymerization. Vinyl neodecanoate-containing polymers are used in decorative emulsion paints, plasters and renders especially in Europe. Vinyl neodecanoate, like most vinyl ester monomers, is very hydrophobic and the structure is highly branched with a tertiary substituted α-carbon. It is used as a hydrophobic co-monomer.

One important property of membrane lipids is their amphipathic character. Amphipathic lipids have a polar, hydrophilic head group and a non-polar, hydrophobic region. The figure to the right shows the inverted cone-like shape of sphingomyelin and the cone-like shape of cholesterol based on the area of space occupied by the hydrophobic and hydrophilic regions. Cholesterol can pack in between the lipids in rafts, serving as a molecular spacer and filling any voids between associated sphingolipids.

The transmembrane region of many integral membrane proteins consists of one or more alpha helices. The orientations and interactions of these helices directly affect cell signaling and molecular transport across the bilayer. The hydrophobic environment of the phospholipid tails in turn modulates the position and structure of such domains and thus may influence protein function. Conversely, the bilayer itself can (locally) change the thickness of its hydrocarbon region to interact optimally with hydrophobic regions of a transmembrane protein (a.k.a.

It forms a homopentameric channel with ten transmembrane spanners. Combining both Ec-MscL molecular model and Tb-MscL crystal structure, it is clear that M1 helices in the core of the transmembrane bundle make up the main gate of the mechanosensitive channel. Regularly placed glycine residues on the M1 segments permits tight packing of the five central helices, forming a narrow (~4 Å) hydrophobic constriction. Hydrophobic M2 helices on the periphery of the MscL barrel face the lipid bilayer.

In the inward facing conformation, the binding site on the A domain is open directly to the surrounding aqueous solutions. This allows hydrophilic molecules to enter the binding site directly from the inner leaflet of the phospholipid bilayer. In addition, a gap in the protein is accessible directly from the hydrophobic core of the inner leaflet of the membrane bilayer. This allows hydrophobic molecules to enter the binding site directly from the inner leaflet of the phospholipid bilayer.

Tachykinins are a family of neuropeptides that share the same hydrophobic C-terminal region with the amino acid sequence Phe-X-Gly-Leu-Met-NH2, where X represents a hydrophobic residue that is either an aromatic or a beta-branched aliphatic. The N-terminal region varies between different tachykinins. The term tachykinin originates in the rapid onset of action caused by the peptides in smooth muscles. SP is the most researched and potent member of the tachykinin family.

However the hydrophobic effect is not considered a non-covalent interaction as it is a function of entropy and not a specific interaction between two molecules, usually characterized by entropy.enthalpy compensation. An essentially enthalpic hydrophobic effect materializes if a limited number of water molecules are restricted within a cavity; displacement of such water molecules by a ligand frees the water molecules which then in the bulk water enjoy a maximum of hydrogen bonds close to four.

A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity. The hydrophobic effect is responsible for the separation of a mixture of oil and water into its two components. It is also responsible for effects related to biology, including: cell membrane and vesicle formation, protein folding, insertion of membrane proteins into the nonpolar lipid environment and protein-small molecule associations. Hence the hydrophobic effect is essential to life.

Released pulmonary surfactant acts as a protective layer to prevent alveolar from collapsing due to surface tension. Furthermore, surfactants also contains some innate immune components to defend against pulmonary infections. Surfactant is classified into two types of proteins, hydrophilic proteins that are responsible for innate immune system, and hydrophobic proteins that carry out physical functions of pulmonary surfactant. Surfactant metabolism dysfunction involves mutations or malfunctions of those hydrophobic proteins that lead to ineffective surfactant layer to protect alveolus integrity.

A table comparing four different scales for the hydrophobicity of an amino acid residue in a protein with the most hydrophobic amino acids on the top A number of different hydrophobicity scales have been developed. There are clear differences between the four scales shown in the table. Both the second and fourth scales place cysteine as the most hydrophobic residue, unlike the other two scales. This difference is due to the different methods used to measure hydrophobicity.

It is the only achiral proteinogenic amino acid. It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. The acyl radical is glycyl.

FTIR is used to investigate proteins in hydrophobic membrane environments. Studies show the ability of FTIR to directly determine the polarity at a given site along the backbone of a transmembrane protein.

The specific peptide bonds cleaved are those on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine. For more on how this is accomplished, see serine protease.

Bactoprenol is a lipid first identified in certain species of lactobacili. It is a hydrophobic alcohol that plays a key role in the growth of cell walls (peptidoglycan) in Gram-positive bacteria.

Organic pollutants such as solvents or pesticides may be rendered unavailable to microorganisms and thus persist in the environment when they are adsorbed to soil minerals or partition into hydrophobic organic matter.

"General Principle of Membrane Protein Folding and Stability". Stephen White Laboratory Homepage. 10 Nov. 2009. web. Membrane proteins which have hydrophobic surfaces, are relatively flexible and are expressed at relatively low levels.

Carboxypeptidase T (, CPT) is an enzyme. This enzyme catalyses the following chemical reaction: : Releases a C-terminal residue, which may be hydrophobic or positively charged. This enzyme is isolated from Thermoactinomyces vulgaris.

The hydrophobic nature of fly ash gives pavements better resistance to stripping. Fly ash has also been shown to increase the stiffness of the asphalt matrix, improving rutting resistance and increasing mix durability.

Hydrophobic interactions in protein SEC are relatively weak at low ionic strength, electrostatic effects may contribute significantly to retention, and this allows us to use an SEC column as a weak ion exchanger.

Capability to encapsulate hydrophilic, hydrophobic, and amphiphilic substance, being simple to prepare, and all the aforementioned qualities give cubosomes a property that can be used in controlled transport applications as drug delivery vehicles.

It contains the EQVSHHPP sequence. It has an hydrophobic pocket that binds a sterol and also contains multiple membrane binding surfaces which permit the protein to have the ability to cause liposome aggregation.

Sec14p exhibits two distinct domains, made up of twelve ⍺-helices, six 𝛽-strands, and eight 310-helices. The phospholipid binding domain of Sec14p consists of a hydrophobic pocket within the carboxy-terminal domain.

The domain itself adopts an all-α protein fold, a bundle of four alpha helices each separated by loop regions of variable lengths that form a hydrophobic pocket that recognizes the acetyl lysine.

In the search for a substance that fit the criteria mentioned, the crystal structure of imatinib bound to Abl was examined. This revealed a hydrophobic pocket around the phenyl ring adjacent to the piperazinylmethyl group of imatinib. Attempts to utilize this pocket to increase efficacy led to the addition of various hydrophobic groups including single fluoro, bromo and chloro substituents. Finally a trifluoromethyl group at position 3 was found to give the best results, with approximately 36-fold improvement over imatinib.

Chymosin is used to bring about the extensive precipitation and curd formation in cheese-making. The native substrate of chymosin is K-casein which is specifically cleaved at the peptide bond between amino acid residues 105 and 106, phenylalanine and methionine. The resultant product is calcium phosphocaseinate. When the specific linkage between the hydrophobic (para-casein) and hydrophilic (acidic glycopeptide) groups of casein is broken, the hydrophobic groups unite and form a 3D network that traps the aqueous phase of the milk.

Thus, the sample is applied to the column in a buffer which is highly polar. The eluant is typically an aqueous buffer with decreasing salt concentrations, increasing concentrations of detergent (which disrupts hydrophobic interactions), or changes in pH. In general, Hydrophobic Interaction Chromatography (HIC) is advantageous if the sample is sensitive to pH change or harsh solvents typically used in other types of chromatography but not high salt concentrations. Commonly, it is the amount of salt in the buffer which is varied.

Many workers were satisfied with empirical descriptions of specific systems rather than attempt a mechanistic model of the process, and it is possibly for this reason that the adoption of the technology has been slow despite its enormous potential. Foam fractionation is closely related to the allied process of froth flotation in which hydrophobic particles attach to the surface of bubbles which rise to form a pneumatic (i.e. rising) foam. In this way, relatively hydrophobic particles can be separated from relatively hydrophilic particles.

Subunit C consists of hydrophobic membrane-spanning, primarily helical segments and is the site of quinol oxidization. In some fumarate reductase structures, one or more heme groups are additionally bound to the C subunit and participate in the electron transfer. The D subunit contains hydrophobic alpha helices that span the membrane, but does not participate in the catalytic action of the enzyme. It may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.

These modified PAHs are amphiphilic, which means that they have parts that are both hydrophilic and hydrophobic. When in solution, they assemble in discotic mesogenic (liquid crystal) stacks which, like lipids, tend to organize with their hydrophobic parts protected. On February 21, 2014, NASA announced a greatly upgraded database for tracking polycyclic aromatic hydrocarbons (PAHs) in the universe. More than 20% of the carbon in the universe may be associated with PAHs, possible starting materials for the formation of life.

Hydrophobic portion of protein can act as "wedge" when inserting into lipid bilayer. Epsin is one example that utilizes this mechanism to drive membrane bending. Epsin has several amphipathic alpha helices that allows it to partition between the hydrophobic core of the membrane and surrounding aqueous, hydrophilic environment. Another interesting characteristic of epsin and other proteins that bind to membranes is the fact that it shows high binding affinity for a fairly common membrane lipid, phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2).

The primary structure (string of amino acids) of a protein ultimately encodes its uniquely folded three-dimensional (3D) conformation. The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. Folding is driven by the burial of hydrophobic side chains into the interior of the molecule so to avoid contact with the aqueous environment. Generally proteins have a core of hydrophobic residues surrounded by a shell of hydrophilic residues.

In the context of pharmacodynamics (what a drug does to the body), the hydrophobic effect is the major driving force for the binding of drugs to their receptor targets. On the other hand, hydrophobic drugs tend to be more toxic because they, in general, are retained longer, have a wider distribution within the body (e.g., intracellular), are somewhat less selective in their binding to proteins, and finally are often extensively metabolized. In some cases the metabolites may be chemically reactive.

The presence or absence of O chains determines whether the LPS is considered rough or smooth. Full-length O-chains would render the LPS smooth, whereas the absence or reduction of O-chains would make the LPS rough. Bacteria with rough LPS usually have more penetrable cell membranes to hydrophobic antibiotics, since a rough LPS is more hydrophobic. O antigen is exposed on the very outer surface of the bacterial cell, and, as a consequence, is a target for recognition by host antibodies.

Noncovalent solid-phase organic synthesis or NC-SPOS is a form of Solid-phase synthesis whereby the organic substrate is bonded to the solid phase not by a covalent bond but by other chemical interactions. This bond may consist of an induced dipole interaction between a hydrophobic matrix and a hydrophobic anchor. As long as the reaction medium is hydrophilic (polar) in nature the anchor will remain on the solid phase. Switching to a nonpolar solvent releases the organic substrate containing the anchor.

If a substance has properties that do not allow it to overcome these strong intermolecular forces, the molecules are precipitated out from the water. Contrary to the common misconception, water and hydrophobic substances do not "repel", and the hydration of a hydrophobic surface is energetically, but not entropically, favorable. When an ionic or polar compound enters water, it is surrounded by water molecules (hydration). The relatively small size of water molecules (~ 3 angstroms) allows many water molecules to surround one molecule of solute.

Mitochondrial and many bacterial SQRs are composed of four structurally different subunits: two hydrophilic and two hydrophobic. The first two subunits, a flavoprotein (SdhA) and an iron-sulfur protein (SdhB), form a hydrophilic head where enzymatic activity of the complex takes place. SdhA contains a covalently attached flavin adenine dinucleotide (FAD) cofactor and the succinate binding site and SdhB contains three iron-sulfur clusters: [2Fe-2S], [4Fe-4S], and [3Fe-4S]. The second two subunits are hydrophobic membrane anchor subunits, SdhC and SdhD.

Another example, the western grebe, performs a mating ritual that includes running across the surface of water. Surface living animals such as the water strider typically have hydrophobic feet covered in small hairs that prevent the feet from breaking the surface and becoming wet. Another insect known to walk on the water surface is the ant species Polyrhachis sokolova. The pygmy gecko (Coleodactylus amazonicus), due to its small size and hydrophobic skin is also able to walk on the water surface.

A lack of or mutation in CSQ2 has been directly associated with catecholaminergic polymorphic ventricular tachycardia (CPVT). A mutation can have a significant effect if it disrupts the linear polymerization ability of CASQ2, which directly accounts for its high-capacity to bind Ca2+. In addition, the hydrophobic core of domain II appears to be necessary for CASQ2's function, because a single amino acid mutation that disrupts this hydrophobic core directly leads to molecular aggregates, which are unable to respond to calcium ions.

Passive systems employ hydrophobic surfaces. Appropriately designed textiles, characterised by a high level of water resistance and natural self-cleaning effect can stop the adhesion of waterAryeh Ben-Na'im Hydrophobic Interaction Plenum Press, New York, , thereby eliminating ability for ice build-up. Another passive system makes use of the amount of time that a water drop needs to be in touch with frozen material before the drop freezes and sticks. Rough surfaces, with ridges shorten the time that water stays in contact.

The hydration layer plays a vital role in sustaining solubility and suitable natural conformation. There are three main protein- water interaction: ion hydration between charged side chains, hydrogen bonding between polar groups and water, and hydrophobic hydration. Once salt is added to the mixture, there is an increase in the surface tension of the water, thus increasing hydrophobic interactions between water and the protein of interest. The protein of interest then reduces its surface area, which diminishes its contact with the solvent.

Tachykinins are a family of neuropeptides that share the same hydrophobic C-terminal region with the amino acid sequence Phe-X-Gly-Leu-Met-NH2, where X represents a hydrophobic residue that is either an aromatic or a beta-branched aliphatic. The N-terminal region varies between different tachykinins. The term tachykinin originates in the rapid onset of action caused by the peptides in smooth muscles. Substance P (SP) is the most researched and potent member of the tachykinin family.

Transmembrane helices are visible in structures of membrane proteins determined by X-ray diffraction. They may also be predicted on the basis of hydrophobicity scales. Because the interior of the bilayer and the interiors of most proteins of known structure are hydrophobic, it is presumed to be a requirement of the amino acids that span a membrane that they be hydrophobic as well. However, membrane pumps and ion channels also contain numerous charged and polar residues within the generally non-polar transmembrane segments.

The chemical structure and charge distribution of atractyloside is similar to that of ADP: the sulfate groups correspond to the phosphate groups, the glucose part corresponds to the ribose part, and the hydrophobic atractyligenine residue corresponds to the hydrophobic purine residue of ADP. The carboxyl group on the C4 atom of the atractyligenin is important for toxicity. If this is reduced to a hydroxyl group (atractylitriol), the substance becomes non-toxic. Modification of any of the sulfate groups renders the compound non-toxic.

For example, a simple routine of coating cotton fabric with silica or titania particles by sol-gel technique has been reported, which protects the fabric from UV light and makes it superhydrophobic. Similarly, silica nanoparticles can be deposited on top of already hydrophobic carbon fabric. The carbon fabric by itself is identified as inherently hydrophobic, but not distinguished as superhydrophobic since its contact angle is not higher than 150°. With the adhesion of silica nanoparticles, contact angles as high as 162° are achieved.

The method used to obtain the Janin and Rose et al. scales was to examine proteins with known 3-D structures and define the hydrophobic character as the tendency for a residue to be found inside of a protein rather than on its surface. Since cysteine forms disulfide bonds that must occur inside a globular structure, cysteine is ranked as the most hydrophobic. The first and third scales are derived from the physiochemical properties of the amino acid side chains.

For this reason, similar mechanisms and machinery are utilized in cell–cell fusion. In response to certain stimuli, such as low pH or binding to cellular receptors, these fusogens will change conformation. The conformation change allows the exposure of hydrophobic regions of the fusogens that would normally be hidden internally due to energetically unfavorable interactions with the cytosol or extracellular fluid. These hydrophobic regions are known as fusion peptides or fusion loops, and they are responsible for causing localized membrane instability and fusion.

A cake made with egg yolks would not be as light and airy because they have a lower foaming ability than egg whites. This move, to the air/water interface, by the proteins is also aided by their hydrophobic and hydrophilic part. The hydrophobic moieties orient themselves toward the air while the hydrophilic moieties orient themselves toward the water portion of the interface. The air molecules at the air/water interface interact less with the other molecules that are fully inside the bubble.

By extended storage in the dark, water is replaced by oxygen and hydrophilicity is once again lost. A significant majority of hydrophobic surfaces have their hydrophobic properties imparted by structural or chemical modification of a surface of a bulk material, through either coatings or surface treatments. That is to say, the presence of molecular species (usually organic) or structural features results in high contact angles of water. In recent years, rare earth oxides have been shown to possess intrinsic hydrophobicity.

Liquid marbles were first reported by P. Aussillous and D. Quere in 2001, who described a new method to construct portable water droplets in the atmospheric environment with hydrophobic coating on their surface to prevent the contact between water and the solid ground (Figure 1). Liquid marbles provide a new approach to transport liquid mass on the solid surface, which sufficiently transform the inconvenient glass containers into flexible, user-specified hydrophobic coating composed of powders of hydrophobic materials. Since then, the applications of liquid marbles in no-loss mass transport, microfluidics and microreactors have been extensively investigated. However, liquid marbles only reflect the water behavior at the solid-air interface, while there is no report on the water behavior at the liquid-liquid interface, as a result of the so-called coalescence cascade phenomenon.

The NDUFB10 protein weighs 21 kDa and is composed of 172 amino acids. NDUFB10 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

The NDUFB6 protein weighs 15.5 kDa and is composed of 128 amino acids. NDUFB6 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

Cytochrome c was also discovered in 1996 by Dr. Xiaodong Wang to have an intermediate role in apoptosis, a controlled form of cell death used to kill cells in the process of development or in response to infection or DNA damage. Cytochrome c binds to cardiolipin in the inner mitochondrial membrane, thus anchoring its presence and keeping it from releasing out of the mitochondria and initiating apoptosis. While the initial attraction between cardiolipin and cytochrome c is electrostatic due to the extreme positive charge on cytochrome c, the final interaction is hydrophobic, where a hydrophobic tail from cardiolipin inserts itself into the hydrophobic portion of cytochrome c. During the early phase of apoptosis, mitochondrial ROS production is stimulated, and cardiolipin is oxidized by a peroxidase function of the cardiolipin–cytochrome c complex.

Instead, the Pagano laboratory found that cyclin F is the substrate receptor of an SCF ubiquitin ligase that ubiquitinates and directly interacts with downstream targets, such as CP110 and RRM2, through its hydrophobic patch.

In HgeTx1, it seems likely that the Lys24 residue will interact with the hydrophobic Met33 or Leu34 residue according to the functional dyad model, which allows it to block the Shaker B K+-channel.

The Protein Binding Theory suggests that a narcotic binds to receptors on the hydrophobic region of cellular membrane proteins. In both theories, the cell membranes are targeted by narcotics resulting in decreased functionality, narcosis.

The hydrophobic core of the bilayer is typically 3-4 nm thick, but this value varies with chain length and chemistry. Core thickness also varies significantly with temperature, in particular near a phase transition.

Stathmin, and the related proteins SCG10 and XB3, contain a N-terminal domain (XB3 contains an additional N-terminal hydrophobic region), a 78 amino acid coiled-coil region, and a short C-terminal domain.

First, a small aperture is created in a thin layer of a hydrophobic material such as Teflon. Typically the diameter of this hole is a few tens of micrometers up to hundreds of micrometers.

1) has a 12 TMS topology with intracellular N- and C-termini. Two-fold structural symmetry in the arrangement of membrane helices for TM1-5 and TM6-10 (conserved Slc2 hydrophobic core) is suggested.

Impression taken with silicon There are two types of silicone impression material, addition and condensation (reflecting each of their setting reactions). Silicones are inherently hydrophobic and as such require excellent moisture control for optimal use.

They are hydrophobic and act on membrane receptors. ;Steroid: Steroid hormones are derived from cholesterol. Examples include the sex hormones estradiol and testosterone as well as the stress hormone cortisol. Steroids contain four fused rings.

Galactose is bound in the center of the core, occluded from the outside solutions by hydrophobic residues. The architecture of the core is similar to that of the leucine transporter (LeuT) (TC# 2.A.22.4.

The C5bC6 complex is bound by C7. This junction alters the configuration of the protein molecules exposing a hydrophobic site on C7 that allows the C7 to insert into the phospholipid bilayer of the pathogen.

These tubes have the polar head groups facing out, and the hydrophobic hydrocarbon chains facing the interior. This phase is only seen under unique, specialized conditions, and most likely is not relevant for biological membranes.

400 mbar), compared to the ambient. The hot steam flows to the first evaporation–condensation stage (stage 1). Evaporation–condensation stages: Stages are composed of alternative hydrophobic membrane and foil (Polypropylene, PP) frames. Feed (e.g.

The macrocycle envelops the ion with a hydrophobic sheath, which facilitates phase transfer properties. The potassium (K+) complex of the macrocycle 18-crown-6 . Macrocycles are often bioactive and could be useful for drug delivery.

Gold nanoparticles are being investigated as carriers for drugs such as Paclitaxel. The administration of hydrophobic drugs require molecular encapsulation and it is found that nanosized particles are particularly efficient in evading the reticuloendothelial system.

The methyl ester content in orange juice determines hydrophobic character, which is favored at low water activity.KLAVONS, JEROME A., BENNETT RD. "Preparation of Alkyl Esters of Pectin and Pectic Acid." J. Food Sci., 1995. Web.

In the deinking stage the goal is to release and remove the hydrophobic contaminants from the recycled paper. The contaminants are mostly printing ink and stickies. Several processes are used, most commonly flotation or washing.

A drop on a lotus surface, with a contact angle of greater than 146°. A water droplet falling onto a superhydrophobic, elastic surface. Ultrahydrophobic (or superhydrophobic) surfaces are highly hydrophobic, i.e., extremely difficult to wet.

The crystal structure of esterase from the tobacco hornworm Manduca sexta has been solved in complex with the transition state analogue inhibitor 3-octylthio-1,1,1-trifluoropropan-2-one (OTFP) covalently bound to the active site. This crystal structure contains a long, hydrophobic binding pocket with the solvent-inaccessible catalytic triad located at the end. The structure explains many of the interactions observed between JHE and its substrates and inhibitors, such as the preference for methyl esters vs. ethyl or isopropyl esters, and long hydrophobic backbones.

BAK1 is a pro-apoptotic Bcl-2 protein containing four Bcl-2 homology (BH) domains: BH1, BH2, BH3, and BH4. These domains are composed of nine α-helices, with a hydrophobic α-helix core surrounded by amphipathic helices and a transmembrane C-terminal α-helix anchored to the mitochondrial outer membrane (MOM). A hydrophobic groove formed along the C-terminal of α2 to the N-terminal of α5, and some residues from α8, binds the BH3 domain of other BCL-2 proteins in its active form.

IF central rods contain heptad repeats (repeating seven residue patterns) of hydrophobic resides that allow two different IF proteins to intertwine into a coiled-coil formation via hydrophobic interactions. These heterodimers are formed between specific pairs of type I (acidic) and type II (basic) keratin. K5, a type II keratin, pairs with the type I keratin K14. The coiled-coil dimers undergo stepwise assembly and combine in an antiparallel manner, forming end-to-end interactions with other coiled-coils to form large 10 nm intermediate filaments.

The hydrophobic tails are usually fatty acids that differ in lengths. The interactions of lipids, especially the hydrophobic tails, determine the lipid bilayer physical properties such as fluidity. Membranes in cells typically define enclosed spaces or compartments in which cells may maintain a chemical or biochemical environment that differs from the outside. For example, the membrane around peroxisomes shields the rest of the cell from peroxides, chemicals that can be toxic to the cell, and the cell membrane separates a cell from its surrounding medium.

RNase A is a basic protein (pI = 9.63); its many positive charges are consistent with its binding to RNA (a poly-anion). More generally, RNase A is unusually polar or, rather, unusually lacking in hydrophobic groups, especially aliphatic ones. This may account for its need of four disulfide bonds to stabilize its structure. The low hydrophobic content may also serve to reduce the physical repulsion between highly charged groups (its own and those of its substrate RNA) and regions of low dielectric constant (the nonpolar residues).

The toxin then needs a way to get out of the vesicle and into the neuron cytosol in order for it to act on its target. The low pH of the vesicle lumen causes a conformational change in the toxin, shifting it from a water-soluble form to a hydrophobic form. With the hydrophobic patches exposed, the toxin is able to slide into the vesicle membrane. The toxin forms an ion channel in the membrane that is nonspecific for Na+, K+, Ca2+, and Cl- ions.

Okano’s group expanded on their success by using different modifiers to enhance hydrophobicity through the attachment of butyl methacrylate (BMA), a hydrophobic comonomer. For simplification the resultant polymer has been labeled as IBc (isopropylacrylamide butyl methacrylate copolymer). The polymers were synthesized using radical telomerization with varying BMA content. Where pure PNIPAAm was unable to resolve hydrophobic steroids at any temperature, IBc-grafted silica stationary phases were able to resolve steroid peaks with increasingly retarded retention times in correlation to both increased BMA content and increased temperature.

The measurement of contact angles with the Captive Bubble method could also be useful in the surface analysis of the reverse osmosis membrane for the studying of membrane performances. Through the analysis of contact angles, properties of membranes, such as roughness, can be determined. The roughness of membranes, which indicates the effective surface area, can further lead to the investigation in the hydrophilic and hydrophobic properties of the surface. Through studies, a higher contact angle may correspond to a more hydrophobic surface in membrane analysis.

Furthermore, cyclin binding determines the specificity of the cyclin-CDK complex for particular substrates. Cyclins can directly bind the substrate or localize the CDK to a subcellular area where the substrate is found. Substrate specificity of S cyclins is imparted by the hydrophobic batch (centered on the MRAIL sequence), which has affinity for substrate proteins that contain a hydrophobic RXL (or Cy) motif. Cyclin B1 and B2 can localize Cdk1 to the nucleus and the Golgi, respectively, through a localization sequence outside the CDK-binding region.

In samples taken from the North Pacific Gyre in 1999 by the Algalita Marine Research Foundation, the mass of plastic exceeded that of zooplankton by a factor of six. Toxic additives used in plastic manufacturing can leach into their surroundings when exposed to water. Waterborne hydrophobic pollutants collect and magnify on the surface of plastic debris, thus making plastic more deadly in the ocean than it would be on land. Hydrophobic contaminants bioaccumulate in fatty tissues, biomagnifying up the food chain and pressuring apex predators and humans.

Quinoxaline derivatives with a diaryl-amide or diaryl-urea substructure have B-Raf mutant kinase inhibition activity. Some novel quinazoline derivatives inhibit Raf kinase selectively and have less effect on inhibition of VEGFR-2 and EGFR kinase. A scaffold in position N1 on quinolone and quinazoline derivatives behaves as a hydrogen bond receptor and interacts with Cys919 residue. The terminal substituent aromatic ring can form hydrophobic bonds with the hydrophobic pocket of VEGFR-2, especially the terminal phenyl group substituted by chloride in the para-position.

Such microbial mats are modern analogs to stromatolites: Precambrian laminated sedimentary rocks, which are the oldest known microfossils (dated to be 3.5 billion years old). During the last decade of his life, Shilo’s work focused on benthic cyanobacteria. Production of a hydrophobic external surface allows these organisms to adhere to submerged surfaces. Spreading through a planktonic phase occurs by formation of special cells that have a hydrophilic surface and detach from the mother cells, or transient secretion of substances that mask the hydrophobic surface .

Ideally, sphingomyelin molecules are shaped like a cylinder, however many molecules of sphingomyelin have a significant chain mismatch (the lengths of the two hydrophobic chains are significantly different). The hydrophobic chains of sphingomyelin tend to be much more saturated than other phospholipids. The main transition phase temperature of sphingomyelins is also higher compared to the phase transition temperature of similar phospholipids, near 37 C. This can introduce lateral heterogeneity in the membrane, generating domains in the membrane bilayer. Sphingomyelin undergoes significant interactions with cholesterol.

Diagram of the arrangement of amphipathic lipid molecules to form a lipid bilayer. The yellow polar head groups separate the grey hydrophobic tails from the aqueous cytosolic and extracellular environments. Lipid bilayers form through the process of molecular self-assembly. The cell membrane consists primarily of a thin layer of amphipathic phospholipids that spontaneously arrange so that the hydrophobic "tail" regions are isolated from the surrounding water while the hydrophilic "head" regions interact with the intracellular (cytosolic) and extracellular faces of the resulting bilayer.

After binding to lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria, polymyxins disrupt both the outer and inner membranes. The hydrophobic tail is important in causing membrane damage, suggesting a detergent-like mode of action. Removal of the hydrophobic tail of polymyxin B yields polymyxin nonapeptide, which still binds to LPS, but no longer kills the bacterial cell. However, it still detectably increases the permeability of the bacterial cell wall to other antibiotics, indicating that it still causes some degree of membrane disorganization.

Microbial produced surfactants, i.e. biosurfactants reduce the interfacial tension between water and oil, and therefore a lower hydrostatic pressure is required to move the liquid entrapped in the pores to overcome the capillary effect. Secondly, biosurfactants contribute to the formation of micelles providing a physical mechanism to mobilise oil in a moving aqueous phase. Hydrophobic and hydrophilic compounds are in play and have attracted attention in MEOR research, and the main structural types are lipopeptides and glycolipids, being the fatty acid molecule the hydrophobic part.

In the bulk aqueous phase, surfactants form aggregates, such as micelles, where the hydrophobic tails form the core of the aggregate and the hydrophilic heads are in contact with the surrounding liquid. Other types of aggregates can also be formed, such as spherical or cylindrical micelles or lipid bilayers. The shape of the aggregates depends on the chemical structure of the surfactants, namely the balance in size between the hydrophilic head and hydrophobic tail. A measure of this is the hydrophilic-lipophilic balance (HLB).

This C-terminal region spans the last 150 amino acids of the HSF1 protein and contains 2 TADs (TAD1 and TAD2). TAD1, which sits at amino acids 401-420, is largely hydrophobic and is predicted to take on an alpha-helical conformation. TAD1 has been shown to directly interact with target DNA to direct HSF1's transcriptional activation. The structure of TAD2, amino acids 431-529, is not expected to be helical as it contains proline residues in addition to hydrophobic and acidic ones.

Dynamic hydrogen bonds between molecules of liquid water The origin of the hydrophobic effect is not fully understood. Some argue that the hydrophobic interaction is mostly an entropic effect originating from the disruption of highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute. A hydrocarbon chain or a similar nonpolar region of a large molecule is incapable of forming hydrogen bonds with water. Introduction of such a non- hydrogen bonding surface into water causes disruption of the hydrogen bonding network between water molecules.

A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules (i.e. exerts chaotropic activity). This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules (proteins, nucleic acids) by weakening the hydrophobic effect. For example, a chaotropic agent reduces the amount of order in the structure of a protein formed by water molecules, both in the bulk and the hydration shells around hydrophobic amino acids, and may cause its denaturation.

Similar hydrofuge surfaces are known in other insects, including aquatic insects that spend most of their lives submerged, with hydrophobic hairs preventing entry of water into their respiratory system. Some birds are great swimmers, due to their hydrophobic feather coating. Penguins are coated in a layer of air and can release that trapped air to accelerate rapidly when needing to jump out of the water and land on higher ground. Wearing an air coat when swimming reduces the drag and also acts as a heat insulator.

Surfactant is a surface-active lipoprotein complex formed by type II alveolar cells. The proteins and lipids that comprise surfactant have both a hydrophilic region and a hydrophobic region. By absorbing to the air-water interface of alveoli with the hydrophilic head groups in the water and the hydrophobic tails facing towards the air, the main lipid component of surfactant, dipalmitoylphosphatidylcholine, reduces surface tension. It also means the rate of shrinking is more regular because of the stability of surface area caused by surfactant.

Thermopsin () is an enzyme. This enzyme catalyses the following chemical reaction : Similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1' This enzyme is isolated from the thermophilic archeaon Sulfolobus acidocaldarius.

Molecular Cell Biology. 5th ed. W.H. Freeman and Company New York, 2004. 535–539. The phospholipid bilayer is a two-layer structure mainly composed of phospholipids, which are amphiphilic molecules that have hydrophilic and hydrophobic regions.

Hence it presents a limitation that the inner and outer tube surfaces are identical. Molecular assembly mostly occurs through weak non-covalent bonds which includes: hydrogen bonds, ionic bonds, van der Waals interactions, and hydrophobic interactions.

For dipping starting from below the liquid surface, the substrate should by hydrophilic, and for dipping starting above the liquid surface, the substrate should be hydrophobic. Multilayers can be achieved by successive dipping through alternating monolayers.

The dual targeted proteins have a more hydrophobic targeting peptide than both mitochondrial and chloroplastic ones. However, it is tedious to predict if a peptide is dual-targeted or not based on its physico-chemical characteristics.

Polystyrene is used as a medium for ion- exchange. It is made from the polymerization of styrene with the use of divinylbenzene and benzoyl peroxide. Such exchangers form hydrophobic interactions with proteins which can be irreversible.

The energetics of DNA tertiary structure assembly were determined to be driven by the hydrophobic effect, in addition to Watson-Crick base pairing, which is responsible for sequence selectivity, and stacking interactions between the aromatic bases.

With hydrophilic fibres like cotton, wool, polyamide and polyacrylonitrile, sodium triphosphate removes soil more effectively than a surfactant alone. With hydrophobic fibres like polyesters and polyolefins, the effectiveness of the surfactant surpasses that of the builder.

Also, often the hydrophobic properties matter. Thereby, NSAIs activity is mostly dependent on the size and shape of the drug structure along with steric characteristics and interaction of the azole group to the heme prosthetic group .

Journal of Immunology. 161: 4356-4365. It is due to the greater hydrophobic interactive properties displayed by PZP in comparison with tetrameric α2M, that functions of PZP such as holdase-type chaperone activity have been suggested.

It does this by forming weak, transient bonds with nucleoporins at their various FG (Phe-Gly) motifs. Crystallographic analysis has shown that these motifs bind to importin-β at shallow hydrophobic pockets found on its surface.

Cry34Ab1 is unrelated to Bt delta-endotoxins. It is an aegerolysin () composed of two beta sheets in a beta-sandwich structure; the total protein is composed of 117 amino acid residues and contains a hydrophobic core.

The NDUFA4L2 gene is located on the long q arm of chromosome 12 at position 13.3 and it spans 5,860 base pairs. NDUFA4L2 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

The water-soluble proteins tend to have their hydrophobic residues (Leu, Ile, Val, Phe, and Trp) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. (Note that in biochemistry, a residue refers to a specific monomer within the polymeric chain of a polysaccharide, protein or nucleic acid.) The integral membrane proteins tend to have outer rings of exposed hydrophobic amino acids that anchor them into the lipid bilayer. Some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that locks onto the membrane. In similar fashion, proteins that have to bind to positively charged molecules have surfaces rich with negatively charged amino acids like glutamate and aspartate, while proteins binding to negatively charged molecules have surfaces rich with positively charged chains like lysine and arginine.

Tropoelastin aggregates at physiological temperature due to interactions between hydrophobic domains in a process called coacervation. This process is reversible and thermodynamically controlled and does not require protein cleavage. The coacervate is made insoluble by irreversible crosslinking.

It is also connected to the SDHC/SDHD subunits on the hydrophobic end of the complex anchored in the mitochondrial membrane. The subunit is an iron-sulfur protein with three iron-sulfur clusters. It weighs 30 kDa.

Although regular concrete can be re-crushed, it involves a very costly process, which often means that the concrete ends up in a landfill. This advantage of hydrophobic concrete enables its cost-efficient reuse in future projects.

Silicone films can be applied to such silica-based substrates as glass to form a covalently bonded hydrophobic coating. Many fabrics can be coated or impregnated with silicone to form a strong, waterproof composite such as silnylon.

Metal salts of naphthenic acids, which are called naphthenates, are widely used as hydrophobic sources of metal ions in diverse applications.M. Landau. 1993. "Driers and metallic soaps", in J. Kroschwitz, ed., Kirk-Othmer Encyclopedia of Chemical Technology.

This process in tablet or capsule formulations enhance the disintegration of the drug/excipient bulk and so enhance the rate of dissolution of the hydrophobic drug. Examples of the hydrophilic polymers are methyl cellulose and hydroxyethyl cellulose.

Casein contains a high number of proline residues, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. It is relatively hydrophobic, making it poorly soluble in water.

In brief, binding site identification usually relies on identification of concave surfaces on the protein that can accommodate drug sized molecules that also possess appropriate "hot spots" (hydrophobic surfaces, hydrogen bonding sites, etc.) that drive ligand binding.

Surface sizing solutions consist of mainly modified starches and sometimes other hydrocolloids, such as gelatine, or surface sizing agents such as acrylic co-polymers. Surface sizing agents are amphiphilic molecules, having both hydrophilic (water-loving) and hydrophobic (water-repelling) ends. The sizing agent adheres to substrate fibers and forms a film, with the hydrophilic tail facing the fiber and the hydrophobic tail facing outwards, resulting in a smooth finish that tends to be water-repellent. Sizing improves the surface strength, printability, and water resistance of the paper or material to which it is applied.

It plays a role in the biogenesis of tight junctions and in the establishment of cell polarity in epithelial cells. Each L27_N domain consists of three alpha-helices, the first two of which form an antiparallel coiled-coil. Two L27 domains come together to form a four-helical bundle with the antiparallel coiled-coils formed by the first two helices. The third helix of each domain forms another coiled-coil packing at one end of the four-helix bundle, creating a large hydrophobic interface: the hydrophobic interactions are the major force that drives heterodimer formation.

The α-helical rod domain contains repeating segments of hydrophobic amino acids, such that the first and fourth residues of every set of seven amino acids are usually nonpolar. This specific structure enables two intermediate filament polypeptides to coil together and create a "hydrophobic seal". The rod also contains specific placement of alternating acidic and basic residues, many of which are spaced 4 amino acids apart. This spacing is optimal for the formation of ionic salt bridges, which serve to stabilize the α-helical rod through intrachain interactions.

The exact structure and composition of the crystals used in hydrophobic concrete is not public information; due to its properties, however, it can be assumed that it is a non-polar molecule. The property to repel water gives hydrophobic concrete the ability to avoid contamination by particles dissolved in water drops. Because the crystals themselves are not polar, there is little interaction between the crystals and dissolved oxygen. This allows the concrete to withstand the rebar rusting that so often compromises the strength of concrete that has iron bars running through it.

This domain has a similar composition to thioredoxins, which act as antioxidants by facilitating the reduction of other proteins. In comparison, the region that contains the greatest amount of variability between GST classes is contained in the alpha-2 helix on the C-terminal domain. The predominantly alpha-helical C-terminal domain is involved with the binding of hydrophobic substrates (such as hydrophobic portions of xenobiotics). The specificity of the alpha-2 helix stems from the assortment of amino acids in the domain that interacts with the glycine residue of glutathione.

Ara h 1 is a vicilin, located in the protein fraction of the peanut cotyledon. Ara h 1 forms homotrimers, and due to its highly stable structure, mediated through hydrophobic interactions, it has been established as an allergen. Hydrophobic residues on α-helical bundles are located on the ends of each trimer monomer. Ara h 1 presents an overall pleat like bicupins, N- and C-terminal domains are superposed in 1.9 Å. The molecule has two modules related by an axis perpendicular to the three pleat axes of the trimer.

The particular chemical depends on the nature of the mineral to be recovered and, perhaps, the natures of those that are not wanted. As an example, sodium ethyl xanthate may be added as a collector in the selective flotation of galena (lead sulfide) to separate it from sphalerite (zinc sulfide). This slurry (more properly called the pulp) of hydrophobic particles and hydrophilic particles is then introduced to tanks known as flotation cells that are aerated to produce bubbles. The hydrophobic particles attach to the air bubbles, which rise to the surface, forming a froth.

Thenoyltrifluoroacetone, C8H5F3O2S, is a chemical compound used pharmacologically as a chelating agent. It is an inhibitor of cellular respiration by blocking the respiratory chain at complex II. Perhaps the first report of TTFA as an inhibitor of respiration was by A. L. Tappel in 1960. Tappel had the (erroneous) idea that inhibitors like antimycin and alkyl hydroxyquinoline-N-oxide might work by chelating iron in the hydrophobic milieu of respiratory membrane proteins, so he tested a series of hydrophobic chelating agents. TTFA was a potent inhibitor, but not because of its chelating ability.

A membrane-spanning, solvent-accessible channel runs along the sevenfold axis and ranges from 14 Å to 46 Å in diameter. On the exterior of the 14-strand antiparallel β barrel there is a hydrophobic belt approximately 30 Å in width that provides a surface complementary to the nonpolar portion of the lipid bilayer. The interfaces are composed of both salt-links and hydrogen bonds, as well as hydrophobic interactions, and these contacts provide a molecular stability for the heptamer in SDS solutions even up to 65 °C.

Shape of a self-splicing intron with two exons (shown in red and blue). DS Goodsell, 2005, PDB At Yale, Doudna's group was able to crystallize and solve the three-dimensional structure of the catalytic core of the Tetrahymena Group I ribozyme. They showed that a core of five magnesium ions clustered in one region of the P4-P6 domain of the ribozyme, forming a hydrophobic core around which the rest of the structure could fold. This is analogous, but chemically distinct from, the way proteins typically have a core of hydrophobic amino acids.

The molecules of an antistatic agent often have both hydrophilic and hydrophobic areas, similar to those of a surfactant; the hydrophobic side interacts with the surface of the material, while the hydrophilic side interacts with the air moisture and binds the water molecules. Internal antistatic agents are designed to be mixed directly into the material, external antistatic agents are applied to the surface. Common antistatic agents are based on long-chain aliphatic amines (optionally ethoxylated) and amides, quaternary ammonium salts (e.g., behentrimonium chloride or cocamidopropyl betaine), esters of phosphoric acid, polyethylene glycol esters, or polyols.

Triton X-100 structure Detergents are organic amphipathic (with hydrophobic tail and a hydrophilic head) surfactants. They are used to separate membrane proteins from membrane because the hydrophobic part of detergent can surround biological membranes and thus isolate membrane proteins from membranes. Although detergents are widely used and have similar functions, it is important to understand the physical and chemical properties of the detergents of interest in order to determine the optimal one to use for your experiment. Detergents are often categorized as nonionic, anionic, cationic, or zwitterionic, based on their hydrophilic head group feature.

When synthesized to have alternating regions of hydrophobic and hydrophilic monomers, copolymers can stabilize the suspension because their hydrophobic group adsorbs strongly to the colloid surface while the hydrophilic group is attracted to the solvent. In general, the adsorption of polymers to clay surfaces is entropically favored because one polymer molecule displaces many water molecules which were previously bound to the soil particle. Polymer and clay particle suspensions have been used to understand the mechanism of this steric stabilization in soils. Consider a homopolymer adsorbed to the surfaces of clay particles in suspension.

In place of solvent gradient elution, thermoresponsive polymers allow the use of temperature gradients under purely aqueous isocratic conditions. The versatility of the system is controlled not only through changing temperature, but through the addition of modifying moieties that allow for a choice of enhanced hydrophobic interaction, or by introducing the prospect of electrostatic interaction. These developments have already introduced major improvements to the fields of hydrophobic interaction chromatography, size exclusion chromatography, ion exchange chromatography, and affinity chromatography separations as well as pseudo-solid phase extractions ("pseudo" because of phase transitions).

The gene encoding MscL protein is trkA and it is located in the inner membrane of the E. coli. The protein is 17 KDa, and consists of 136 amino acids; mostly hydrophobic residues resulting in two hydrophobic segments, however molecular weight of the functional channel is presumed to be 60-70 KDa from gel filtration experiments, suggesting oligomerization. As a common feature no cysteines residues are present in this channel. In 1998 the homolog MscL from mycobacterium tuberculosis Tb-MscL was elucidated at closed state by X ray crystallography at 3.5 Å resolution.

This behavior allows considering amphiphilic Janus nanoparticles as analogues of molecular surfactants for the stabilization of emulsions. In 2005, spherical silica particles with amphiphilic properties were prepared by partial modification of the external surface with an alkylsilane agent. These particles form spherical assemblies encapsulating water-immiscible organic compounds in aqueous media by facing their hydrophobic alkylsilylated side to the inner organic phase and their hydrophilic side to the outer aqueous phase, thus stabilizing oil droplets in water. In 2009, hydrophilic surface of silica particles was made partially hydrophobic by adsorbing cetyltrimethylammonium bromide.

ALPS motifs are 20 to 40 amino acid long portions of proteins that have important collections of types of amino acid residues. Bulky hydrophobic amino acid residues, such as Phenylalanine, Leucine, and Tryptophan are present every 3 or 4 positions, with many polar but uncharged amino acid residues such as Glycine, Serine and Threonine between. The ALPS is unstructured in solution but folds as an alpha helix when associated with the membrane bilayer, such that the hydrophobic residues insert between loosely packed lipids and the polar residues point toward the aqueous cytoplasm.

In addition to recognizing amino acids, ubiquitin ligases can also detect unusual features on substrates that serve as signals for their destruction. For example, San1 (Sir antagonist 1), a nuclear protein quality control in yeast, has a disordered substrate binding domain, which allows it to bind to hydrophobic domains of misfolded proteins. Misfolded or excess unassembled glycoproteins of the ERAD pathway, on the other hand, are recognized by Fbs1 and Fbs2, mammalian F-box proteins of E3 ligases SCFFbs1and SCFFbs2. These recognition domains have small hydrophobic pockets allowing them to bind high-mannose containing glycans.

The interactions involved in gelation and aggregation of casein micelles are hydrogen bonds, hydrophobic interactions, electrostatic attractions and van der Waals attractions These interactions are highly dependent on pH, temperature and time. At the isoelectric point, the net surface charge of casein micelle is zero and a minimum of electrostatic repulsion can be expected. Furthermore, aggregation is taking place due to dominating hydrophobic interactions. Differences in the zeta potential of milk can be caused by differences in ionic strength differences, which in turn depend on the amount of calcium present in the milk.

Hydrophobic forces are the attractive entropic forces between any two hydrophobic groups in aqueous media, e.g. the forces between two long hydrocarbon chains in aqueous solutions. The magnitude of these forces depends on the hydrophobicity of the interacting groups as well as the distance separating them (they are found to decrease roughly exponentially with the distance). The physical origin of these forces is a debated issue but they have been found to be long-ranged and are the strongest among all the physical interaction forces operating between biological surfaces and molecules.

Pluronic P123 is a symmetric triblock copolymer comprising poly(ethylene oxide) (PEO) and poly(propylene oxide) (PPO) in an alternating linear fashion, PEO-PPO-PEO. The unique characteristic of PPO block, which is hydrophobic at temperatures above 288 K and is soluble in water at temperatures below 288 K, leads to the formation of micelle consisting of PEO-PPO-PEO triblock copolymers. Some studies report that the hydrophobic core contains PPO block, and a hydrophilic corona consists of PEO block. In 30wt% aqueous solution Pluronic P123 forms a cubic gel phase.

After initiation, elongation, and termination, there is a fourth step of the disassembly of the post-termination complex of ribosome, mRNA, and tRNA, which is a prerequisite for the next round of protein synthesis. The large ribosomal subunit has a role in protein folding both in vitro and in vivo. The large ribosomal subunit provides a hydrophobic surface for the hydrophobic collapse step of protein folding. The newly synthesized protein needs full access to the large subunit to fold; this process may take a period of time (5 minutes for beta-galactosidase).

Many MHC class I alleles prefer hydrophobic C-terminal residues, and the immunoproteasome complex is more likely to generate hydrophobic C-termini. Due to its role in generating the activated form of NF-κB, an anti-apoptotic and pro-inflammatory regulator of cytokine expression, proteasomal activity has been linked to inflammatory and autoimmune diseases. Increased levels of proteasome activity correlate with disease activity and have been implicated in autoimmune diseases including systemic lupus erythematosus and rheumatoid arthritis. The proteasome is also involved in Intracellular antibody-mediated proteolysis of antibody-bound virions.

Molecular chaperones are typically referred to as proteins that associate with and help other proteins reach a native conformation while not being present in the end state. Chaperones bind to their substrate (i.e. a misfolded protein) in an ATP-dependent manner to perform a specific function. Exposed hydrophobic residues are a major problem with regards to protein aggregation because they can interact with one another and form hydrophobic interactions. It is the job of chaperones to prevent this aggregation by binding to the residues or providing proteins a “safe” environment to fold properly.

Because the intracellular space is very crowded, sometimes proteins need an isolated space to prevent aberrant interactions between other proteins, which is provided by chaperonins or HSP60s . HSP60s are barrel shaped and suited to bind to the hydrophobic residues of proteins. Once a cap binds to the chaperonin, the protein is free within the barrel to undergo hydrophobic collapse and reach a stable conformation. Once the cap is removed, the protein can either be correctly folded and move on to perform its function or return to a HSP if it is still not folded accurately.

The digestive enzyme α-amylase is responsible for the breakdown of the starch molecule into maltotriose and maltose, which can be used as sources of energy. Amylose is also an important thickener, water binder, emulsion stabilizer, and gelling agent in both industrial and food-based contexts. Loose helical amylose chains have a hydrophobic interior that can bind to hydrophobic molecules such as lipids and aromatic compounds. The one problem with this is that, when it crystallizes or associates, it can lose some stability, often releasing water in the process (syneresis).

The phospholipids are amphiphilic. The hydrophilic end usually contains a negatively charged phosphate group, and the hydrophobic end usually consists of two "tails" that are long fatty acid residues. In aqueous solutions, phospholipids are driven by hydrophobic interactions that result in the fatty acid tails aggregating to minimize interactions with water molecules. The result is often a phospholipid bilayer: a membrane that consists of two layers of oppositely oriented phospholipid molecules, with their heads exposed to the liquid on both sides, and with the tails directed into the membrane.

The most common location of α helices is at the surface of protein cores, where they provide an interface with the aqueous environment. The inner-facing side of the helix tends to have hydrophobic amino acids and the outer-facing side hydrophilic amino acids. Thus, every third of four amino acids along the chain will tend to be hydrophobic, a pattern that can be quite readily detected. In the leucine zipper motif, a repeating pattern of leucines on the facing sides of two adjacent helices is highly predictive of the motif.

Hydrophobic inhibitors like rotenone or piericidin most likely disrupt the electron transfer between the terminal FeS cluster N2 and ubiquinone. It has been shown that long-term systemic inhibition of complex I by rotenone can induce selective degeneration of dopaminergic neurons. Complex I is also blocked by adenosine diphosphate ribose – a reversible competitive inhibitor of NADH oxidation – by binding to the enzyme at the nucleotide binding site. Both hydrophilic NADH and hydrophobic ubiquinone analogs act at the beginning and the end of the internal electron- transport pathway, respectively.

Amphipols (a portmanteau of amphiphilic polymers) are a class of amphiphilic polymers designed to keep membrane proteins soluble in water without the need for detergents, which are traditionally used to this end but tend to be denaturing. Amphipols adsorb onto the hydrophobic transmembrane surface of membrane proteins thanks to their hydrophobic moieties and keep the complexes thus formed water-soluble thanks to the hydrophilic ones. Amphipol-trapped membrane proteins are, as a rule, much more stable than detergent-solubilized ones, which facilitates their study by most biochemical and biophysical approaches. Popot, J.-L.

This indicates that mucin segments extend into the ambient solution at a long distance. Because mucin is amphiphilic, the non-glycosylated regions of the molecule interacts with the surface and the glycosylated region interacts with the ambient solution causing the steric repulsion. The repulsive forces applied by the mucin creates anti-adhesive properties which can suppress cell adhesion to surfaces. The efficiency of mucin adherence to hydrophobic surfaces has been analyzed by applying a coating of mucin and measuring the number of mucins remaining on the hydrophobic material after rinsing.

A plot of chain length vs. the logarithm of the lipid bilayer/buffer partition coefficient K is linear, with the addition of each methylene group causing a change in the Gibbs free energy of -3.63 kJ/mol. The cutoff effect was first interpreted as evidence that anaesthetics exert their effect not by acting globally on membrane lipids but rather by binding directly to hydrophobic pockets of well-defined volumes in proteins. As the alkyl chain grows, the anaesthetic fills more of the hydrophobic pocket and binds with greater affinity.

Typically directional selection acts strongly for short bursts and is not sustained over long periods of time. If it did, a population might hit biological constraints such that it no longer responds to selection. However, it is possible for directional selection to take a very long time to find even a local optimum on a fitness landscape. A possible example of long-term directional selection is the tendency of proteins to become more hydrophobic over time, and to have their hydrophobic amino acids more interspersed along the sequence.

There is also a 'second shell' of hydrogen bonding involving residues that interact with the first shell residues. However, the streptavidin-biotin affinity exceeds that which would be predicted from the hydrogen bonding interactions alone, suggesting another mechanism contributing to the high affinity. The biotin-binding pocket is hydrophobic, and there are numerous van der Waals force-mediated contacts and hydrophobic interactions made to the biotin when in the pocket, which is also thought to account for the high affinity. In particular, the pocket is lined with conserved tryptophan residues.

Emerin is a 29.0 kDa (34 kDa observed MW) protein composed of 254 amino acids. Emerin is a serine-rich protein with an N-terminal 20-amino acid hydrophobic region that is flanked by charged residues; the hydrophobic region may be important for anchoring the protein to the membrane, with the charged terminal tails being cytosolic. In cardiac, skeletal, and smooth muscle, emerin localizes to the inner nuclear membrane; expression of emerin is highest in skeletal and cardiac muscle. In cardiac muscle specifically, emerin also resides at adherens junctions within intercalated discs.

Both agonists and antagonists are known to form hydrogen bonds with His297. It can be concluded that interactions with the amino acid residues, Asp147 and Tyr148 are essential for the ligand to bind to the receptor and the molecules that form additional polar interactions with other residues are more often antagonists than agonists. The N-substituent group can form hydrophobic bonds with Tyr326 and Trp293 and the aromatic and cyclohexane rings can form similar bonds to Met151. The backside of the ligand can also form a hydrophobic bond, but with Val300 and Ile296.

Two of these disulfide bridges contribute to maintaining the relative position of one of the β-sheet and α-helix. The third disulfide bridge binds the long loop between the first β-sheet and α-helix to the C-terminus, while the fourth binds this loop to the third β-sheet. The Cn2 peptide contains many aromatic residues: seven tyrosine residues, two tryptophan residues and one phenylalanine residue. These residues form two hydrophobic patches, a hydrophobic core, two positive patches, and a negative patch in the protein, which have been extensively described.

The activation of water is facilitated by proton abstraction via the catalytic triad between a water molecule, glutamine, and histidine. After hydrolysis, the substrate is then released from its bond to the aspartic acid residue, liberating the diol product from the enzyme active site. 350x350px The active site of this enzyme lies within a hydrophobic pocket in the enzyme, which in turn leads to the enzyme's preferential reactivity with molecules with hydrophobic side-chains. The mEH enzyme typically binds to small organic epoxides, such as styrene epoxide and cis-stillbene-oxide.

In aqueous solutions, micelles are assemblies of amphipathic molecules with their hydrophilic heads exposed to solvent and their hydrophobic tails in the center. Micelles can solubilize membrane proteins by partially encapsulating them and shielding their hydrophobic surfaces from solvent. Bicelles are a related class of model membrane, typically made of two lipids, one of which forms a lipid bilayer while the other forms an amphipathic, micelle-like assembly shielding the bilayer center from surrounding solvent molecules. Bicelles can be thought of as a segment of bilayer encapsulated and solubilized by a micelle.

Hydrophilic sub-regions of κ-casein are cleaved off, leaving behind largely hydrophobic aggregate. The enzymes thus destabilize κ-casein micelles and encourage clumping of hydrophobic protein residues, causing milk to curdle. Major industrial drawbacks of rennet include its limited supply and high cost, its inaccessibility to vegetarians and practicing members of certain religious groups, and recent European national bans on utilization of recombinant calf rennet. Fungal proteases are largely unsuitable as rennet substitutes, and enzymes from many plant extracts have been shown to produce low yields, poor textures, and bitter flavors of cheese.

Thiele et al. explored the possibilities of a cellulose-based material that could be responsive to humidity. They developed a bilayer film using cellulose steraroyl esters with different substitution degrees on either side. One ester had a substitution degree of 0.3 (highly hydrophilic) and the other had a substitution degree of 3 (highly hydrophobic.) When the sample was cooled from 50 °C to 22 °C, and the relative humidity increased from 5.9% to 35%, the hydrophobic side contracted and the hydrophilic side swelled, causing the sample to roll up tightly.

When there are changes in the non-covalent interactions, as may happen with a change in the amino acid sequence, the protein is susceptible to misfolding or unfolding. In these cases, if the cell does not assist the protein in re-folding, or degrade the unfolded protein, the unfolded/misfolded protein may aggregate, in which the exposed hydrophobic portions of the protein may interact with the exposed hydrophobic patches of other proteins. There are three main types of protein aggregates that may form: amorphous aggregates, oligomers, and amyloid fibrils.

After removal of excess water - also to avoid hydrolysis of the AKD to the beta-keto acid and subsequent decarboxylation to the ketone - Hydrolyse von Alkylketendimeren zu beta-Ketosäuren und Decarboxylierung zum Keton follows the cracking of the stabilized AKD particles on the base paper mass, the melting of the solid AKD wax (at approx. 90 °C), the spreading of the liquid AKD wax by surface diffusion on the cellulose fibers and the formation of closed hydrophobic layers. The thickness of the hydrophobic layers depends on the AKD concentration in the dispersion. Ad 3.

Bafetinib in its binding site Due to the structural similarities of imatinib and bafetinib, their binding to Bcr-Abl is also quite similar. The only notable difference comes from the hydrophobic interaction between the trifluoromethyl group and the hydrophobic pocket created by Ile-293, Leu-298, Leu-354, and Val-379. This group can also be linked to bafetinib's specificity for Lyn, as the binding site there is almost identical to that on Bcr-Abl. Bafetinib is effective both against most imatinib resistant mutations (not including T315I) and some dasatinib resistant mutations.

Pancreatic elastase is a compact globular protein with a hydrophobic core. This enzyme is formed by three subunits. Each subunit binds one calcium ion (cofactor). There are three important metal-binding sites in amino acids 77, 82, 87.

The process is accomplished by vigorous mixing of the hydrophobic drug with the aqueous solution of the hydrophilic polymer solution, leading to production of small particles of the drug covered with small droplets of the hydrophilic polymer solution.

When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all-β-sheet structure with exposed hydrophobic regions. This causes the protein to aggregate and cause the solidification associated with cooked egg white.

However, deleting the translocation region of amino acids decreases the cytotoxic activity 4-fold. Both cysteine proteases and a majority of translocation regions harbor hydrophobic proteins, which show access to TcdB and other toxins crossing the cell membranes.

There are several examples in which displacement chromatography has been applied to the purification of proteins using ion exchange, hydrophobic interaction, as well as reversed-phase chromatography.R. Freitag and J. Breier. J. Chromatogr. A 691, 101–112 (1995).

The function of SRP was discovered by the study of processed and unprocessed immunoglobulin light chains; newly synthesized proteins in eukaryotes carry N-terminal hydrophobic signal sequences, which are bound by SRP when they emerge from the ribosome.

Octadecyltrimethoxysilane (OTMS) is an organosilicon compound. This colorless liquid is used for preparing hydrophobic coatings and self-assembled monolayers. It is sensitive toward water, irreversibly degrading to a siloxane polymer. It places a C18H39SiO3 "cap" on oxide surfaces.

By using the ppOD films, the hydrophilic polar Si-OH groups in the polymer itself are concealed by non-polar CxHy hydrocarbon groups, so when it's applied as a film to the silica particles, they become hydrophobic as well.

The other, alternatively spliced form expressed primarily in the erythroid tissues, differs at the C-terminus, and contains a cleavable hydrophobic peptide with a PI-anchor site. It associates with membranes through the phosphoinositide (PI) moieties added post- translationally.

GPR endopeptidase (, germination proteinase) is an enzyme. This enzyme catalyses the following chemical reaction: : Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala This enzyme participates in spore germination in Bacillus megaterium.

ArsA and ArsB form an anion-translocating ATPase. The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.

Like other silanols, trimethylsilanol is being tested for use as an antimicrobial agent. TMS is used for hydrophobic coating on silicate surfaces. It reacts with the silanol groups (R3SiOH) of the substrate, resulting in a layer of methyl groups.

Hydrophilization is a process used for hydrophobic drugs to increase their release rate from capsules, which is dependent on the rate of dissolution, by covering the surface of the drug particles with minute droplets of a hydrophilic polymer solution.

Soil compaction is also impacts infiltration capacity. Compaction of soils results in decreased porosity within the soils, which decreases infiltration capacity. Hydrophobic soils can develop after wildfires have happened, which can greatly diminish or completely prevent infiltration from occurring.

The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.

Electrowetting is the modification of the wetting properties of a hydrophobic surface with an applied electric field. Electrowetting is now used in a wide range of applications from modulab to adjustable lenses, electronic displays and switches for optical fibers.

The biggest drawbacks to using these techniques relate to the chemistry of the technique itself and its lack of sensitivity. As they rely on PAGE gels, extremely large, small, highly hydrophobic, acidic, or basic molecules will not be visualized.

Streptopain (, Streptococcus peptidase A, streptococcal cysteine proteinase, Streptococcus protease) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage with hydrophobic residues at P2, P1 and P1' This enzyme is isolated from the bacterium, group A Streptococcus.

The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds.

The NDUFB7 protein weighs 16.4 kDa and is composed of 137 amino acids. NDUFB7 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. NDUFB7 and NDUFB8 have been shown to localize at the intermembrane surface of complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

The NDUFB8 protein weighs 22 kDa and is composed of 186 amino acids. NDUFB8 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. NDUFB7 and NDUFB8 have been shown to localize at the intermembrane surface of complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two- domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

The catalytic domain of PDE3 is characterized by a 44-amino acid insert, but this insert is unique to the PDE3 family, and is a factor when determining a structure for a potent and selective PDE3 inhibitor. The crystal structure of the catalytic domains of several PDEs, including PDE3B, have shown that they contain three helical subdomains: # N-terminal cyclin fold region # Linker region # C-terminal helical bundle At the interface of these domains a deep hydrophobic pocket is formed by residues that are highly conserved among all PDEs. This pocket is the active site and is composed of four subsites : # Metal binding site (M site) # Core pocket (Q pocket) # Hydrophobic pocket (H pocket) # Lid region (L region) The M site is at the bottom of the hydrophobic binding pocket and contains two divalent metal binding sites. The metal ions that can bind to these sites are either zinc or magnesium.

The phospholipid bilayer that forms the cell surface membrane consists of a hydrophobic inner core region sandwiched between two regions of hydrophilicity, one at the inner surface and one at the outer surface of the cell membrane (see lipid bilayer article for a more detailed structural description of the cell membrane). The inner and outer surfaces, or interfacial regions, of model phospholipid bilayers have been shown to have a thickness of around 8 to 10 Å, although this may be wider in biological membranes that include large amounts of gangliosides or lipopolysaccharides. The hydrophobic inner core region of typical biological membranes may have a thickness of around 27 to 32 Å, as estimated by Small angle X-ray scattering (SAXS). The boundary region between the hydrophobic inner core and the hydrophilic interfacial regions is very narrow, at around 3Å, (see lipid bilayer article for a description of its component chemical groups).

A yeast two-hybrid screen revealed that Bck2 physically interacts with Mcm1, Swi4, Yap6, and Mot3. A V69E mutation on a hydrophobic pocket in Mcm1 prevents binding of Yox1 and Fkh2. This same mutation resulted in loss of interaction with Bck2.

Only few hydrophobic unnatural base as a fifth base significantly augment the aptamer affinity to target proteins. As a resource for all in vitro selection and SELEX experiments, the Ellington lab has developed the Aptamer Database cataloging all published experiments.

Mycolysin (, pronase component, Streptomyces griseus neutral proteinase, actinase E, SGNPI) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with hydrophobic residues in P1' This enzyme is present in Streptomyces griseus, S. naraensis, and S. cacaoi.

Second, the narrow and reduced hydrophobic rim on the surface of the β –barrel causes local destabilization of the outer membrane. Third, ability to undergo lateral opening of the barrel by transient separation of 1st and 16th β–barrel strands.

Very-low-density lipoproteins transport endogenous triglycerides, phospholipids, cholesterol, and cholesteryl esters. It functions as the body's internal transport mechanism for lipids. In addition it serves for long-range transport of hydrophobic intercellular messengers, like the morphogen Indian hedgehog (protein).

The salicylic acid portion of the molecule absorbs ultraviolet rays with a wavelength from 295 nm to 315 nm, protecting the skin from sun damage. The hydrophobic trimethyl cyclohexane functional group provides greasiness that prevents it from dissolving in water.

A helix corner, also called an alpha-alpha corner, has two alpha helices almost at right angles to each other connected by a short 'loop'. This loop is formed from a hydrophobic residue. The function of a helix corner is unknown.

Principle of the photoelectrowetting effect Photoelectrowetting is a modification of the wetting properties of a surface (typically a hydrophobic surface) using incident light.S. Arscott, 'Moving liquids with light: Photoelectrowetting on semiconductors', Sci. Rep. 1, 184, (2011). Scientific Reports: Nature Publishing Group.

The oxidized form also exposes more hydrophobic areas and possesses a larger cleft to facilitate substrate binding. P4HB has been shown to dimerize in vivo via noncatalytic bb' domains. Formation of dimer blocks substrate- binding site and inhibits P4HB’s activity.

The globular structure of bacteriocin AS-48 consists of five alpha helices enclosing a hydrophobic core. The mammalian NK- lysin effector protein of T and natural killer cells has a similar structure, though it lacks sequence homology with bacteriocins AS-48.

The substrate binding site is long, thin and hydrophobic and kinks the substrate tail at the location where the di-iron catalytic centre introduces the double bond. dimer with the major ligand??citation??, Stearyl-CoA (magenta), docked to the active site.

A.77) together. These proteins are all of about the same size and apparent topology, further suggesting a common evolutionary origin. The leucine exporter homologue (YeaS or LeuE; TC# 2.A.76.1.5) exports leucine and several other neutral, hydrophobic amino acids.

Geldanamycin is hydrophobic. Outer particle diameter varied from than less 500 to 750 µm. Alginate formed the shell of capsule and its thickness varied from 30 to 90 µm. Dibutyl sebacate or oleic acid as liquid core extracted geldanamycin well.

Applied at pressures from 0.5 to 5 MPa (5 to 50 atm) to a protein crystal, xenon atoms bind in predominantly hydrophobic cavities, often creating a high-quality, isomorphous, heavy-atom derivative that can be used for solving the phase problem.

The C-terminal of H2A.X contains an additional motif compared to H2A. The motif that is added is Ser-Gln-(Glu/Asp)- (hydrophobic residue). The motif becomes heavily phosphorylated at the serine residue; if this phosphorylation occurs the variant becomes γH2A.

Calcium is a divalent cation, allowing it to form bonds with several caseinate anions. This leads to the formation of several covalent bonds between caseinate anions, which can ultimately cause the cross-linked caseinate to form pockets of hydrophobic regions.

Aqualysin 1 (, caldolysin) is an enzyme. This enzyme catalyses the following chemical reaction : Exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position This enzyme is isolated from the thermophile, Thermus aquaticus.

The ball enters the open channel and binds to the hydrophobic inner vestibule within the channel. This blockage causes inactivation of the channel by stopping the flow of ions. This phenomenon has mainly been studied in potassium channels and sodium channels.

While hydrophobic substances are usually lipophilic, there are exceptions, such as the silicones and fluorocarbons. The term hydrophobe comes from the Ancient Greek ὑδρόφόβος (hýdrophóbos), "having a horror of water", constructed .Liddell, H.G. & Scott, R. (1940). A Greek-English Lexicon.

Composite insulators are less costly, lighter in weight, and have excellent hydrophobic capability. This combination makes them ideal for service in polluted areas. However, these materials do not yet have the long-term proven service life of glass and porcelain.

If the liquid molecules are strongly attracted to the solid molecules then the liquid drop will completely spread out on the solid surface, corresponding to a contact angle of 0°. This is often the case for water on bare metallic or ceramic surfaces, although the presence of an oxide layer or contaminants on the solid surface can significantly increase the contact angle. Generally, if the water contact angle is smaller than 90°, the solid surface is considered hydrophilic and if the water contact angle is larger than 90°, the solid surface is considered hydrophobic. Many polymers exhibit hydrophobic surfaces.

When the centrifugal force is smaller than the surface tension, the liquid flow will be held in the original chamber; when the centrifugal force overbalances the surface tension due to a higher rotating speed, the liquid flow will break the valve and flow into the next chamber. This can be used to control the flow process simply by controlling the rotating speed of the disk. The most commonly used valves include the hydrophilic valve, the hydrophobic valve, the syphon valve and sacrificial valve. As for hydrophilic and hydrophobic valves, the generation of surface tension is almost the same.

Bafetinib in its binding site Due to the structural similarities of imatinib and bafetinib, their binding to Bcr-Abl is also quite similar. The only notable difference comes from the hydrophobic interaction between the trifluoromethyl group and the hydrophobic pocket created by Ile-293, Leu-298, Leu-354, and Val-379. This group can also be linked to bafetinib's specificity for Lyn, as the binding site there is almost identical to that on Bcr-Abl. Bafetinib has its place in TKI therapy as it is effective both against most imatinib resistant mutations (not including T315I) and some dasatinib resistant mutations.

A vimentin monomer, like all other intermediate filaments, has a central α-helical domain, capped on each end by non-helical amino (head) and carboxyl (tail) domains. Two monomers are likely co-translationally expressed in a way that facilitates their formation of a coiled-coil dimer, which is the basic subunit of vimentin assembly. The α-helical sequences contain a pattern of hydrophobic amino acids that contribute to forming a "hydrophobic seal" on the surface of the helix. In addition, there is a periodic distribution of acidic and basic amino acids that seems to play an important role in stabilizing coiled-coil dimers.

The core of gp41 then folds into a six helical bundle (a coiled coil) structure exposing the previously hidden hydrophobic gp41 fusion peptides that are inserted in the host cell membrane allowing fusion to take place. This fusion process is facilitated by the hairpin conformational structure. The inner core of this conformation is 3 NHRs which have hydrophobic pockets that allow it to bind anti-parallel to specific residues on the CHR. The activation process occurs readily, which suggests that the inactive state of gp41 is metastable and the conformational changes allow gp41 to achieve its more stable active state.

Arginine's side chain is amphipathic, because at physiological pH it contains a positively charged guanidinium group, which is highly polar, at the end of a hydrophobic aliphatic hydrocarbon chain. Because globular proteins have hydrophobic interiors and hydrophilic surfaces, arginine is typically found on the outside of the protein, where the hydrophilic head group can interact with the polar environment, for example taking part in hydrogen bonding and salt bridges. For this reason, it is frequently found at the interface between two proteins. The aliphatic part of the side chain sometimes remains below the surface of the protein.

When performing experiments with denaturants, surfactants or other amphiphilic molecules, the microenvironment of the tryptophan might change. For example, if a protein containing a single tryptophan in its 'hydrophobic' core is denatured with increasing temperature, a red-shifted emission spectrum will appear. This is due to the exposure of the tryptophan to an aqueous environment as opposed to a hydrophobic protein interior. In contrast, the addition of a surfactant to a protein which contains a tryptophan which is exposed to the aqueous solvent will cause a blue-shifted emission spectrum if the tryptophan is embedded in the surfactant vesicle or micelle.

The PHLPP isoforms (PH domain and Leucine rich repeat Protein Phosphatases) are a pair of protein phosphatases, PHLPP1 and PHLPP2, that are important regulators of Akt serine-threonine kinases (Akt1, Akt2, Akt3) and conventional/novel protein kinase C (PKC) isoforms. PHLPP may act as a tumor suppressor in several types of cancer due to its ability to block growth factor-induced signaling in cancer cells. PHLPP dephosphorylates Ser-473 (the hydrophobic motif) in Akt, thus partially inactivating the kinase. In addition, PHLPP dephosphorylates conventional and novel members of the protein kinase C family at their hydrophobic motifs, corresponding to Ser-660 in PKCβII.

This property is exploited in the use of so-called "grease pens," which apply a line of grease to the surface of a suspect diamond simulant. Diamond surfaces are hydrophobic when the surface carbon atoms terminate with a hydrogen atom and hydrophilic when the surface atoms terminate with an oxygen atom or hydroxyl radical. Treatment with gases or plasmas containing the appropriate gas, at temperatures of 450 °C or higher, can change the surface property completely. Naturally occurring diamonds have a surface with less than a half monolayer coverage of oxygen, the balance being hydrogen and the behavior is moderately hydrophobic.

Ergtoxin can decrease hERG K+ activity by 50% at a concentration of 10 nM. The binding of Ergtoxin to hERG K+ has been suggested to be dependent on hydrophobic interactions with the channel pore, specifically with a prominently exposed hydrophobic cluster of amino acids (Tyr 14, Phe 36 and Phe 37). It has also been shown that natural oxidation of Met 35 decreases the affinity of the molecule for the hERG K+ channels by three orders of magnitude, suggesting that Met35 is a critical residue for either polypeptide 3D folding or interaction of the toxin with the channel.

Published online 1 September 2005 Another example is the formation of micelles which has a non-lamellar formation in which the hydrophilic region is significantly larger compared to the hydrophobic region. There are various liquid-crystalline phases that can exist in lipids. Liquid- crystalline phases are when the hydrophobic chain regions are not motionless but are allowed to move about freely in a fluid-like melted state. The lamellar phase (Lα) is the most common and dominant phase in lipids and are aligned as stacks of bilayers on top of bilayers oriented in one single direction.

There are various usages of ethanol which include an additive to gasoline, a primary ingredient for food preservation as well as alcoholic beverages and being used for transdermal drug delivery. For example, it can function as an antiseptic in topical creams to kill bacteria by denaturing proteins. Ethanol is an amphiphilic molecule meaning that it has chemical and physical properties associated with hydrophobic and hydrophilic molecules. Although, studies show that when penetrating through the biomembrane its hydrophobic abilities appear to be limited based on its preference to bind closely to the hydrophilic region of the phospholipids.

Glycosylated (GPI-linked) proteins contain a signal sequence, thus directing them to the endoplasmic reticulum (ER). The protein is co-translationally inserted in the ER membrane via a translocon and is attached to the ER membrane by its hydrophobic C terminus; the majority of the protein extends into the ER lumen. The hydrophobic C-terminal sequence is then cleaved off and replaced by the GPI- anchor. As the protein processes through the secretory pathway, it is transferred via vesicles to the Golgi apparatus and finally to the plasma membrane where it remains attached to a leaflet of the cell membrane.

While the secondary structures are determined by energy state and hydrogen bonds formed between amino acids, hierarchical structures are determined by the hydrophobicity of the peptide. Exon 1 encoded peptide is mainly hydrophilic, and is more extended when immersed in water. In contrast, exon 3 encoded peptide contains both hydrophobic and hydrophilic blocks, suggesting the formation of micelles, where the hydrophobic block will cluster on the inside with the hydrophilic portion surrounding it. Thus, a single complete resilin protein, when immersed in water, takes on the structure in which exon 1 encoded segment extends out from the micelle exon 3 encoded peptide forms.

These peptides are approximately 5 nm in size and have 16 amino acids. The class of Lego peptides has the unique characteristics of having two distinct surfaces being either hydrophobic or hydrophilic, similar to the pegs and holes of Lego blocks. The hydrophobic side promotes self-assembly in water and the hydrophilic sides has a regular arrangement of charged amino acids residues, which in turn brings about a defined pattern of ionic bonds. The arrangement of the residues can be classified according to the order of the charges; Modulus I has a charge pattern of “+-+-+-,” modulus II “++--++--“ and modulus III “+++---+++” and so on.

This headpiece contains an F-actin binding domain. Residues K38, E39, K65, 70-73:KKEK, G74, L75 and F76 surround a hydrophobic core and are believed to be involved in the binding of F-actin to villin. Residues E39 and K70 form a salt bridge buried within the headpiece which serves to connect N and C terminals. This salt bridge may also orient and fix the C-terminal residues involved in F-actin binding as in the absence of this salt bridge no binding occurs. A hydrophobic “cap” is formed by residue W64 side chains, which is completely conserved throughout the villin family.

Wing I is usually a heteroaromatic ring and wing II is a phenyl or allyl substituent. Wing I has a functional group at one side of the ring which is capable of accepting and/or donating hydrogen bonds with the main chain of the amino acids Lys-101 and Lys-103. Wing II interacts through π-π interactions with a hydrophobic pocket, formed in most part by the side chains of aromatic amino acids. On the butterfly body a hydrophobic part fills a small pocket which is mainly formed by the side chains of Lys-103, Val-106 and Val-179.

After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino acids interact with the molecules of solvation and allow proteins to form hydrogen bonds with the surrounding water molecules. If enough of the protein surface is hydrophilic, the protein can be dissolved in water. When salt is added to the solution, there is more frequent interaction between solvent molecules and salt ions. As a result, the protein and salt ions compete to interact with the solvent molecules with the result that there are fewer solvent molecules available for interaction with the protein molecules than before.

Tertiary structure refers to the three-dimensional structure of monomeric and multimeric protein molecules. The α-helixes and β-pleated-sheets are folded into a compact globular structure. The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds. The disulfide bonds are extremely rare in cytosolic proteins, since the cytosol (intracellular fluid) is generally a reducing environment.

Internal salt linkages produce thermal stability, and whether cold temperature results in the destabilization of these linkages is unknown. In principle, the free energy of stabilization of soluble globular proteins does not exceed 50-100 kJ/mol. The stabilization is based on the equivalent of few hydrogen bonds, ion pairs, or hydrophobic interactions, even though numerous intramolecular interactions results in stabilization. Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the stabilization of the inner core through hydrophobic interactions, the free energy of stabilization emerges as small difference between large numbers.

Air pressure was then increased, forcing the hydrophobic layer to be pushed into the water, decreasing the contact angle. When the contact angle was at the desired level, a hydrophilic thiol, 3-mercaptopropane-1,2-diol, was added to the water, causing the hydrophilic thiol to competitively replace the hydrophobic thiols, resulting in the formation of amphiphilic Janus nanoparticles. The liquid–liquid and gas–liquid interface methods do have an issue where the nanoparticles can rotate in solution, causing the deposition of silver on more than one face. A liquid–liquid/liquid–solid hybrid interface method was first introduced by Granick et al.

The analysis of the submitochondrial localization of RDH13 indicates its association with the inner mitochondrial membrane. The primary structure of RDH13 contains two hydrophobic segments, 2–21 and 242–261, which are sufficiently long to serve as transmembrane segments; however, as shown in the present study, alkaline extraction completely removes the protein from the membrane, indicating that RDH13 is a peripheral membrane protein. The peripheral association of RDH13 with the membrane further distinguishes this protein from the microsomal retinaldehyde reductases, which are integral membrane proteins that appear to be anchored in the membrane via their N-terminal hydrophobic segments.

The chemical structure of the conventional Neuberg's hydrotropic salts (proto- type, sodium benzoate) consists generally of two essential parts, an anionic group and a hydrophobic aromatic ring or ring system. The anionic group is involved in bringing about high aqueous solubility, which is a prerequisite for a hydrotropic substance. The type of anion or metal ion appeared to have a minor effect on the phenomenon. On the other hand, planarity of the hydrophobic part has been emphasized as an important factor in the mechanism of hydrotropic solubilization To form a hydrotrope, an aromatic hydrocarbon solvent is sulfonated, creating an aromatic sulfonic acid.

TcdB accesses the interior of the cell through clathrin-mediated endocytosis, When toxin B is part of the cytosol, the glucosyltransferase passes through the endosomal membrane, which decreases pH, induces translocation and finally leads to morphological changes of translocation region residues (958–1130). The hydrophobic regions are embedded in the host membrane to form pores that allow glucosyltransferase domains to pass through. When cells are infected with TcdB in an acidic environment, it attenuates toxins and causes shape rearrangements (Fig. 6). As a consequence of acidic pH, TcdB displays clear differences in original fluorescence of tryptophan, susceptibility of proteases, and hydrophobic surfaces.

Relatively small hydrophobic peptides may not be able to integrate into the membrane, and in response adopt an orientation at the membrane surface. The experimental evidence was shown by a fluorescence study on an artificial peptide with a 19 amino acid long hydrophobic sequence of mainly leucines and flanked on both sides with lysines as anchoring residues.Ren, J.; Lew, S.; Wang, Z.; London, E. Biochemistry 1997, 36, 10213-10220. The results indicated that a conversion from a dominant transmembrane to parallel orientation of the peptide could be induced by modulating bilayer thickness via addition of cholesterol or by increasing lipid chain length.

The C terminus contain a LPXTG sequence motif and hydrophobic amino acid segments attached to peptidoglycan. The C-terminal domain has many features which are required to fulfill its role: a proline-rich wall-spanning region, the wall-anchoring LPTXG motif, a hydrophobic transmembrane region and a cytoplasmic tail of positively charged amino acid residues. wo main beta sheets made up of four beta strands each arranged in to a beta-sandwich topology. The C-terminal part of SdrG(276-596) is integral to the folding of the immunoglobulin-like whole to create the docking grooves necessary for Fg binding.

Ethanol extraction is a type of solvent extraction used to extract fragrant compounds directly from dry raw materials, as well as the impure oils or concrete resulting from organic solvent extraction, expression, or enfluerage. Ethanol extracts from dry materials are called tinctures, while ethanol washes for purifying oils and concretes are called absolutes. The impure substances or oils are mixed with ethanol, which is less hydrophobic than solvents used for organic extraction, dissolves more of the oxidized aromatic constituents (alcohols, aldehydes, etc.), leaving behind the wax, fats, and other generally hydrophobic substances. The alcohol is evaporated under low-pressure, leaving behind absolute.

Characteristic of most all TIM barrel domains is the presence of the enzyme's active site in the lower loop regions created by the eight loops that connect the C-termini of the beta strands with the N-termini of the alpha helices. TIM barrel proteins also share a structurally conserved phosphate binding motif, with the phosphate group found in the substrate or cofactors. In each chain, nonpolar amino acids pointing inward from the beta strands contribute to the hydrophobic core of the structure. The alpha helices are amphipathic: their outer (water-contacting) surfaces are polar, while their inner surfaces are largely hydrophobic.

COX assembly in yeast is a complex process that is not entirely understood due to the rapid and irreversible aggregation of hydrophobic subunits that form the holoenzyme complex, as well as aggregation of mutant subunits with exposed hydrophobic patches. COX subunits are encoded in both the nuclear and mitochondrial genomes. The three subunits that form the COX catalytic core are encoded in the mitochondrial genome. Hemes and cofactors are inserted into subunits I & II. The two heme molecules reside in subunit I, helping with transport to subunit II where two copper molecules aid with the continued transfer of electrons.

Surfactants are usually organic compounds that are amphiphilic, meaning they contain both hydrophobic groups (their tails) and hydrophilic groups (their heads). Therefore, a surfactant contains both a water-insoluble (or oil-soluble) component and a water-soluble component. Surfactants will diffuse in water and adsorb at interfaces between air and water or at the interface between oil and water, in the case where water is mixed with oil. The water-insoluble hydrophobic group may extend out of the bulk water phase, into the air or into the oil phase, while the water-soluble head group remains in the water phase.

These include the enzymatic processing of lipids and other hydrophobic substances, membrane anchoring, and the binding and transfer of small nonpolar compounds between different cellular membranes. These proteins may be anchored to the bilayer as a result of hydrophobic interactions between the bilayer and exposed nonpolar residues at the surface of a protein, by specific non-covalent binding interactions with regulatory lipids , or through their attachment to covalently bound lipid anchors. It has been shown that the membrane binding affinities of many peripheral proteins depend on the specific lipid composition of the membrane with which they are associated.

The human gene encoding it was cloned in 1986 and the deduced protein sequence revealed that ApoD is a member of the lipocalin family, small hydrophobic molecule transporters (Drayna et al, 1986). ApoD is 169 amino acids long, including a secretion peptide signal of 20 amino acids. It contains two glycosylation sites (aspargines 45 and 78) and the molecular weight of the mature protein varies from 20 to 32 kDa (see figure 1).Rassart Figure 1 The resolved tertiary structure shows that ApoD is composed of 8 anti-parallel β-strands forming a hydrophobic cavity capable of receiving different ligands.

1.5 J/cm² per Mol for NaCl, 2.5 J/cm² per Mol for (NH4)2SO4), and because the entropy of the analyte-solvent interface is controlled by surface tension, the addition of salts tend to increase the retention time. This technique is used for mild separation and recovery of proteins and protection of their biological activity in protein analysis (hydrophobic interaction chromatography, HIC). Another important factor is the mobile phase pH since it can change the hydrophobic character of the analyte. For this reason most methods use a buffering agent, such as sodium phosphate, to control the pH.

An efficient way to synthesize protein-polymer hybrid nanoparticles is to take advantage of photoinitiated reversible addition−fragmentation chain transfer (RAFT) polymerization-induced self-assembly(PISA) by using multi-RAFT modified bovine serum albumin (BSA) as a macromolecular chain transfer agent. RAFT mediated growth of the PHPMA chains will graft from the BSA-RAFT, and increase the hydrophobicity of the star BSA−PHPMA conjugates. At the critical aggregation concentration, they form nanoparticles due to the hydrophobic interactions. The resulting nanoparticles show excellent encapsulation capability for both hydrophobic and hydrophilic molecules, such as cancer drugs and DNA.

Schematic cross- section showing the theoretical arrangement of lipids in a hydrophobic pore (top) and a hydrophilic pore (bottom). Electroporation allows cellular introduction of large highly charged molecules such as DNA which would never passively diffuse across the hydrophobic bilayer core. This phenomenon indicates that the mechanism is the creation of nm-scale water-filled holes in the membrane. Electropores were optically imaged in lipid bilayer models like droplet interface bilayers and Giant Unilamellar Vesicles, while addition of cytoskeletal proteins such as actin networks to the Giant Unilamellar Vesicles seem to prevent the formation of visible electropores.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA5 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. The protein localizes to the inner mitochondrial membrane as part of the 7 component-containing, water-soluble iron-sulfur protein (IP) fraction of complex I, although its specific role is unknown. It is assumed to undergo post-translational removal of the initiator methionine and N-acetylation of the next amino acid. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form.

A large rectangular water reservoir with a volume of 350 cum.m is preserved in the Southern part of Nebet Tepe. It was built of alternating layers of stones and bricks while the inner walls and the floor were treated with hydrophobic coating.

The interactions between food and pan are very dependent on the material that the pan is made of. Whether or not the pan is hydrophilic or hydrophobic, the heat conductivity and capacity, surface roughness, and more all determine how the food is cooked.

James Kuo is founder, CEO and Chairman of the Board of Salt Lake City-based BioMicro Systems, a company that makes research tools that control fluids by using hydrophilic (water-attracting) and hydrophobic (water-repelling) materials instead disruptive mechanical or electrical components.

Cortifen, also known as cortiphen or kortifen, as well as fencoron, is a synthetic glucocorticoid corticosteroid and cytostatic antineoplastic agent which was developed in Russia for potential treatment of tumors. It is a hydrophobic chlorphenacyl nitrogen mustard ester of 11-deoxycortisol (cortodoxone).

Oseltamivir has a large hydrophobic side chain and the NA must undergo rearrangement to form a pocket for drug binding by rotating aminoacid E276 and bond with R224. Mutations like H274Y, R292K and N294S that affect this forming could reduce the inhibitor's efficiency.

In regards to the amino acid composition of the pore-lining residues within KcsA, the side chains lining the internal pore and cavity are predominantly hydrophobic, but within the selectivity filter polar amino acids are present that contact the dehydrated K+ ions.

Surfaces that recreate properties of shark skin are intended to enable more efficient movement through water. Efforts have been made to produce fabric that emulates shark skin. Surface tension biomimetics are being researched for technologies such as hydrophobic or hydrophilic coatings and microactuators.

The aspartate residue co-ordinates magnesium ions, and the glutamate is essential for ATP hydrolysis. There is considerable variability in the sequence of this motif, with the only invariant features being a negatively charged residue following a stretch of bulky, hydrophobic amino acids.

NCS-1 also contains at least two known protein binding domains, and a large surface exposed hydrophobic crevice containing EF-hands three and four. There is a myristoylation motif at the N-terminus that presumably allows NCS-1 to associate with lipid membranes.

UBA, CUE, UIM, MIU, VHS, GAT, UBAN), while some are all beta domains (e.g. NZF, UBC, WD40) and others are alpha/beta domains (e.g. UBZ, UEV, PFU). Many of the UBDs bind to ubiquitin via a hydrophobic patch centred on Ile44 (i.e.

Conservative mutations result in an amino acid change. However, the properties of the amino acid remain the same (e.g., hydrophobic, hydrophilic, etc.). At times, a change to one amino acid in the protein is not detrimental to the organism as a whole.

These molecules form a spherical particle in which you can pack a hydrophobic drug molecule. Uhrich’s research group investigates two general classes of nanoscale polymeric micelles: amphiphilic star-like macromolecules (ASMs) and amphiphilic scorpion-like macromolecules (AScMs); both systems facilitate drug transport.

Perfluoroheptane, C7F16, (usually referring to the straight chain molecule called n-perfluoroheptane) is a perfluorocarbon.Pubchem (USG) page on perfluoroheptane It is hydrophobic (water-insoluble) and oleophobic (oil- insoluble). It is used in deacidification of paper as a medium carrying powdered magnesium oxide.

Small molecule antagonists of CCR5 bind to a hydrophobic pocket formed by the transmembrane helices of the CCR5 receptor. They are thought to interact with the receptor in an allosteric manner locking the receptor in a conformation that prohibits its co-receptor function.

The hydrophobic membranes (or PP foils) are welded at both sides of the memsys frame. This frame are designed to combine and distribute vapor, feed, non condensable gas and distillate flows. vibration welded as memsys module (e.g. steam raiser, membrane stage and condenser).

Hydrophobic light-activated adhesive (HLAA) is a type of glue that sets in seconds, but only after exposure to ultraviolet light. One biocompatible, biodegradable HLAA is under consideration for use in human tissue repair as a replacement for sutures, staples and other approaches.

Additionally, enzymes in cascades have also shown substrate-driven chemotactic aggregation. Apart from active enzymes, non-reacting molecules also show chemotactic behavior. This has been demonstrated by using dye molecules that move directionally in gradients of polymer solution through favorable hydrophobic interactions.

These clamps (or hydrophobic side chain bridge analogs) are conserved in 3 indole-3-glycerolphosphate synthase TIM barrel orthologs from the bacterial and archaeal kingdoms, implying they arose in their last common ancestor and have been preserved for over a billion years.

In this complex, all polar carbonyl groups point inwards and nonpolar moieties point outwards, thus building up a hydrophobic exterior for the complex and making it soluble in lipid membranes. This is how nonactin is able to transport potassium ions across lipid membranes.

This can also be explained by the structure of cicutoxin, it consists of 17 carbons, which is hydrophobic. It also has 3 double bonds, 2 triple bonds and two hydroxyl groups, which make the toxin very reactive and not easy to excrete.

Structurally, an ionophore contains a hydrophilic center and a hydrophobic portion that interacts with the membrane. Ions are bound to the hydrophilic center and form an ionophore- ion complex. The structure of the ionophore-ion complex has been verified by X-ray crystallography.

A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzymes active site.

This extreme kinking forces the baseless portion of DNA into APE1's active site. This active site is bordered by Phe266, Trp280, and Leu282, which pack tightly with the hydrophobic side of the AP site, discriminating against sites that do have bases.

3 (4): 133–138. doi:10.1111/j.1708-8240.1991.tb00985.x. ISSN 1496-4155. Scanning electron micrograph of the transition between composite resin (C)-adhesive (A), adhesive-hybrid layer (H), and hybrid layer-dentin. The hybrid layer is hydrophobic, acid resistant and tough.

Being hydrophobic, chlordane adheres to soil particles and enters groundwater only slowly, owing to its low solubility (0.009 ppm). It requires many years to degrade. Chlordane bioaccumulates in animals. It is highly toxic to fish, with an of 0.022–0.095 mg/kg (oral).

Aberrant growth signals also increase smARF expression. ARF is a highly basic (pI>12) and hydrophobic protein. Its basic nature is attributed to its arginine content; more than 20% of its amino acids are arginine, and it contains little or no lysine.

The thrombogenicity is due to the proteins in the blood adapting to the hydrophobic environment when they adhere to the coating. This causes an irreversible change for the protein, and the protein remains stuck to the coating allowing for a blood clot to form.

Researchers identified four categories of silk protein types in the silk of D. triton-- aciniform, ampullate, pyriform, and tubuliform. Egg sacs contain two distinct layers, with the outer layer thought to protect eggs from water due to its unique elemental composition and hydrophobic characteristics.

Most authors place the extent of this effect between 5 and 45 cal/(Å2 mol). Note that this surface area pertains to the solute, while the hydrophobic effect is mostly entropic in nature at physiological temperatures and occurs on the side of the solvent.

Freestanding WS2 films can be produced as follows. WS2 is deposited on a hydrophilic substrate, such as sapphire, and then coated with a polymer, such as polystyrene. After dipping the sample in water for a few minutes, the hydrophobic WS2 film spontaneously peels off.

The predicted M protein sequence does not contain any long hydrophobic or nonpolar domains that might promote membrane association. The protein is rich in basic amino acids and contains a highly basic amino terminal domain. The VSV N protein is required to initiate genome synthesis.

Ubiquinone binding is achieved through a deep hydrophobic binding pocket which is a different mode than other UQ-binding proteins such as succinate-Q oxidoreductase. Although ETF-QO is an integral membrane protein, it does not traverse the entire membrane unlike other UQ-binding proteins.

Oleic acid vesicles represent good models of membrane protocells that could have existed in prebiotic times. Electrostatic interactions induced by short, positively charged, hydrophobic peptides containing 7 amino acids in length or fewer, can attach RNA to a vesicle membrane, the basic cell membrane.

Hydrophobic contaminants are also known to bioaccumulate in fatty tissues, biomagnifying up the food chain and putting great pressure on apex predators. Some plastic additives are known to disrupt the endocrine system when consumed, others can suppress the immune system or decrease reproductive rates.

6th ed. New York: W.H. Freeman, 2013. 908. The cholesterol backbone consists of four hydrocarbon rings, three cyclohexane rings and one cyclopentane, that contribute to its insolubility in aqueous environments. However, the hydrophobic nature allows them to readily diffuse through the plasma membrane of cells.

Melittin is a small peptide with no disulfide bridge; the N-terminal part of the molecule is predominantly hydrophobic and the C-terminal part is hydrophilic and strongly basic. In water, it forms a tetramer but it also can spontaneously integrate itself into cell membranes.

Inkjet printing requires coating paper in a hydrophobic polymer, and then selectively placing an ink that etches the polymer to reveal paper. This technique is low cost with high resolution, but is limited by the speed of placing one ink droplet at a time.

These two active sites are connected by a tunnel lined primarily with backbone atoms and hydrophobic, nonpolar amino acid residues. Structural characterization of asparagine synthetase from mammalian sources have been difficult due to the low abundance and instability of the enzyme during purification procedures.

Also known as Complex I, this enzyme is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site.

They form crosslinked networks in the young cell wall. Typically they have two major diagnostic repetitive peptide motifs, one hydrophilic and the other hydrophobic, with potential for crosslinking. Extensins are thought to act as self-assembling amphiphilesRapaport,H. (2006) Ordered peptide assemblies at interfaces.

Unnamed thermal barrier used in cryogenic fuel tanks made up of hydrophobic silica aerogel has low thermal conductivity, density and high specific surface area. It can be used as thermal insulator to manufacture winter clothes and boots of soldiers stationed in extremely cold region.

Capsules also contain water which protects the bacteria against desiccation. They also exclude bacterial viruses and most hydrophobic toxic materials such as detergents. Immunity to one capsule type does not result in immunity to the other types. Capsules also help cells adhere to surfaces.

Rain-X is a synthetic hydrophobic surface-applied product that causes water to bead up and run off surfaces, most commonly used on glass automobile surfaces. The brand has since been extended to a range of automotive and surface care products, including wiper blades.

Hydrophobins are generally found on the outer surface of conidia and of the hyphal wall, and may be involved in mediating contact and communication between the fungus and its environment. Some family members contain multiple copies of the domain. Hydrophobins have been found to be structurally and functionally similar to cerato-platanins, another group of small cysteine-rich proteins, which also contain a high percentage of hydrophobic amino acids, and are also associated with hyphal growth. This family of proteins includes the rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA), these proteins are the main component of the hydrophobic sheath covering the surface of many fungal spores.

A typical amphiphilic flexible surfactant can form aggregates through a self-assembly process that results of specific interactions between the molecules of the amphiphilic mesogen and those of the non-mesogenic solvent. In aqueous media, the driving force of the aggregation is the "hydrophobic effect". The aggregates formed by amphiphilic molecules are characterised by structures in which the hydrophilic head-groups expose their surface to aqueous solution, shielding the hydrophobic chains from contact with water. For most lyotropic systems aggregation occurs only when the concentration of the amphiphile exceeds a critical concentration (known variously as the critical micelle concentration (CMC) or the critical aggregation concentration (CAC)).

PHLPP1 and 2 also dephosphorylate the hydrophobic motifs of two classes of the protein kinase C (PKC) family: the conventional PKCs and the novel PKCs. (The third class of PKCs, known as the atypicals, have a phospho-mimetic at the hydrophobic motif, rendering them insensitive to PHLPP.) The PKC family of kinases consists of 10 isoforms, whose sensitivity to various second messengers is dictated by their domain structure. The conventional PKCs can be activated by calcium and diacylglycerol, two important mediators of G protein-coupled receptor signaling. The novel PKCs are activated by diacylglycerol but not calcium, while the atypical PKCs are activated by neither.

Energy plays a very important role in p3 peptides. While Aβ models have a strong negative energy, p3 oligomeric models have a positive one. Another characteristic that must be pointed out is that p3 peptides have more solvent-exposed hydrophobic surfaces (60%) than Aβ oligomers do (20%), so buried surface areas are not as big within p3 oligomers (30%) as they are within Aβ oligomers. These evidences show that the expected energy of the Aβ-based oligomeric models of p3 is always positive and that these models expose hydrophobic patches to the solvent and bury a small proportion of their accessible surface within the oligomeric intermediates.

Chymotrypsin (, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin.

In the context of pharmacokinetics (what the body does to a drug), the distribution coefficient has a strong influence on ADME properties of the drug. Hence the hydrophobicity of a compound (as measured by its distribution coefficient) is a major determinant of how drug-like it is. More specifically, for a drug to be orally absorbed, it normally must first pass through lipid bilayers in the intestinal epithelium (a process known as transcellular transport). For efficient transport, the drug must be hydrophobic enough to partition into the lipid bilayer, but not so hydrophobic, that once it is in the bilayer, it will not partition out again.

Peptoid nanosheets have a very high surface area, which can be readily functionalized to serve as a platform for sensing and templating.Olivier, G.K.; Cho, A.; Sanii, B.; Connolly, M.D.; Tran, H.; Zuckermann, R.N. "Antibody-mimetic peptoid nanosheets for molecular recognition" ACS Nano. 7, 9276-9386, (2013). Also, their hydrophobic interiors can accommodate hydrophobic small molecule cargos, which have been demonstrated by the sequestration of Nile red when this dye was injected into an aqueous solution of the peptoid nanosheets.Tran, H., Gael, S.L., Connolly, M.D., Zuckermann, R.N. “Solid-phase submonomer synthesis of peptoid polymers and their self-assemble into highly-ordered nanosheets” J. Vis. Exp.

In a side view, the channel has an hourglass shape, with a cytoplasmic funnel that is empty, and an extracellular funnel that is filled with a little helix, called the plug. In the middle of the membrane is a construction, formed from a pore ring of six hydrophobic amino acids that project their side chains inwards. During protein translocation, the plug is moved out of the way, and a polypeptide chain is moved from the cytoplasmic funnel, through the pore ring, the extracellular funnel, into the extracellular space. Hydrophobic segments of membrane proteins exit sideways through the lateral gate into the lipid phase and become membrane-spanning segments.

The amidine group on NAPAP forms a bidentate salt bridge with Asp deep in the S1 pocket, the piperidine group takes the role of proline residue and binds in the S2 pocket, and the naphthyl rings of the molecule forms a hydrophobic interaction with Trp in the S4 pocket. Pharmaceutical companies have used the structural knowledge of NAPAP to develop DTIs. Dabigatran, like NAPAP binds to S1, S2 and S4 pockets. Benzamidine group on the dabigatran structure binds deep in the S1 pocket, the methylbenzimidazole fits nicely in the hydrophobic S2 pocket and the Ile and Leu at the bottom of the S4 pocket binds to the aromatic group of dabigatran.

Action of bile salts in digestion Recycling of the bile Bile or gall acts to some extent as a surfactant, helping to emulsify the lipids in food. Bile salt anions are hydrophilic on one side and hydrophobic on the other side; consequently, they tend to aggregate around droplets of lipids (triglycerides and phospholipids) to form micelles, with the hydrophobic sides towards the fat and hydrophilic sides facing outwards. The hydrophilic sides are negatively charged, and this charge prevents fat droplets coated with bile from re-aggregating into larger fat particles. Ordinarily, the micelles in the duodenum have a diameter around 1–50 μm in humans.

In line with this, the average length of transmembrane segment of single-span plasma membrane proteins typically is five amino acids longer than the average length of proteins from the Golgi.Bretscher, M.S.; Munro, S. Science 1993, 261, 1280-1281. Experimental evidence was obtained that protein sorting in the Golgi may be based on this length difference: for several proteins that normally reside in the Golgi, it was shown that increasing their hydrophobic length can reroute the proteins to the plasma membrane, or vice versa, that decreasing the hydrophobic length of proteins from the plasma membrane can cause their retention in the Golgi.Munro, S. EMBO J. 1995, 14, 4659-4704.

Two monomers(left and right) are shown and the coenzyme PLP is placed in the crevice between the two domains. Two Dimers: Two monomers of hSDS (human SDH) come together to make a dimer. The interface between the two monomers is formed through hydrogen bonds and hydrophobic interactions. The monomer–monomer contacts involve six pairs of hydrogen bonds formed between 10 residues (Arg98-Asn260, Leu310-Asn260, and Leu265-Lys263). Additional interactions include a number of hydrophobic contacts between the residues Met17, Lys21, Asn101, Glu102, Ser306, Ile308, Ser309, and Ile264 in each monomer. (Figure 2). File:PLPmoleculeSDH.jpg Figure 2 shows the PLP coenzyme situated in the active site of SDH.

Lidocaine has multiple inhibitory actions on the receptor and analysis of the structure of lidocaine has identified the presence of a hydrophobic aromatic ring and a hydrophilic terminal amine. Diethylamine (DEA), a molecule that mimics the hydrophilic moiety of lidocaine by way of a positively charged amine, has been found to block the channel when the receptor is open restricting the flow of Na+ and K+ ions. 2,6-Dimethylaniline (DMA), a molecule that mimics the hydrophobic moiety of lidocaine, has been found to bind the receptor at inter-subunit crevices of the trans-membrane spanning domain thereby causing non-competitive inhibition and restricting the channel from opening.

Coiled-coil α helices are highly stable forms in which two or more helices wrap around each other in a "supercoil" structure. Coiled coils contain a highly characteristic sequence motif known as a heptad repeat, in which the motif repeats itself every seven residues along the sequence (amino acid residues, not DNA base-pairs). The first and especially the fourth residues (known as the a and d positions) are almost always hydrophobic; the fourth residue is typically leucine this gives rise to the name of the structural motif called a leucine zipper, which is a type of coiled-coil. These hydrophobic residues pack together in the interior of the helix bundle.

Ethidium bromide's intense fluorescence after binding with DNA is probably not due to rigid stabilization of the phenyl moiety, because the phenyl ring has been shown to project outside the intercalated bases. In fact, the phenyl group is found to be almost perpendicular to the plane of the ring system, as it rotates about its single bond to find a position where it will impinge upon the ring system minimally. Instead, the hydrophobic environment found between the base pairs is believed to be responsible. By moving into this hydrophobic environment and away from the solvent, the ethidium cation is forced to shed any water molecules that were associated with it.

PLX4720 has good affinity for the ATP binding site partially because its anchor region, a 7-azaindole bicyclic, only differs from the natural adenine that occupies the site in two places where nitrogen atoms have been replaced by carbon. This enables strong intermolecular interactions like N7 hydrogen bonding to C532 and N1 hydrogen bonding to Q530 to be preserved. Excellent fit within the ATP-binding hydrophobic pocket (C532, W531, T529, L514, A481) increases binding affinity as well. Ketone linker hydrogen bonding to water and difluoro-phenyl fit in a second hydrophobic pocket (A481, V482, K483, V471, I527, T529, L514, and F583) contribute to the exceptionally high binding affinity overall.

Synthesis of smart stimuli responsive polysiloxanes through the addition of a polysiloxane amine to an α,β-unsaturated carbonyl via aza-Michael addition to create a polysiloxane with N-isopropyl amide side-chains has been reported. This polysiloxane was shown to be able to load ibuprofen (a hydrophobic NSAID) and then release it in response to changes in temperature, showing it to be a promising candidate for smart drug delivery of hydrophobic drugs. This action was attributed to the polymer's ability to retain the ibuprofen above the lower critical solution temperature (LCST), and conversely, to dissolve below the LCST, thus releasing the loaded ibuprofen at a given, known temperature.

This is also directly applicable to the hydrophobic region in lipid bilayers; if a critical concentration of a chaotropic solute is reached (in the hydrophobic region of the bilayer) then membrane integrity will be compromised, and the cell will lyse. Chaotropic salts that dissociate in solution exert chaotropic effects via different mechanisms. Whereas chaotropic compounds such as ethanol interfere with non-covalent intramolecular forces as outlined above, salts can have chaotropic properties by shielding charges and preventing the stabilization of salt bridges. Hydrogen bonding is stronger in non-polar media, so salts, which increase the chemical polarity of the solvent, can also destabilize hydrogen bonding.

The human TIMM8A gene codes for a translocase involved in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial inner membrane. It is also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. It acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins.

The mechanism(s) by which microorganisms are killed and/or inactivated by defensins is not understood completely. However, it is generally believed that killing is a consequence of disruption of the microbial membrane. The polar topology of defensins, with spatially separated charged and hydrophobic regions, allows them to insert themselves into the phospholipid membranes so that their hydrophobic regions are buried within the lipid membrane interior and their charged (mostly cationic) regions interact with anionic phospholipid head groups and water. Subsequently, some defensins can aggregate to form 'channel-like' pores; others might bind to and cover the microbial membrane in a 'carpet-like' manner.

Aplog-1, a simple and less hydrophobic analog of aplysiatoxin, is a PKC ligand with little tumor-promoting activity that showed growth-inhibitory activities against several cancer cell lines. Multiple derivatives were evaluated for their antiproliferative activity against several human cancer cell lines and binding activity for PKCδ, which plays a tumor suppressor role and is involved in apoptosis. The results showed that the dimethyl groups at position 6 are indispensable to these activities, but that the hydroxyl group at position 18 is not necessary. Of note, the more hydrophobic 12,12-dimethyl-aplog-1 did not show any tumor-promoting activity in vitro or in vivo.

Micelles refers to a type of supramolecular structure consisting of amphiphilic molecules self-assemblies, usually hollow centered. Researchers successfully conjugated a diblock copolymer site specifically onto GFP, the resulting amphiphilic polymer-protein conjugate is capable of reversible self-assembly into micelles. In addition to retaining the native globular shape of proteins, the polypeptide backbone of denatured proteins can also be utilized to be conjugated with hydrophilic polymer chains to generate higher ordered structure through hydrophobic interactions. For example, nanoconjugates of poly-ethylene glycol(PEG) and denatured bovine serum albumin(BSA) will spontaneously self-assemble into a micellar structure, whose protein core can adsorb high numbers of hydrophobic drugs.

Non-biologic surface coatings will occur via two mechanisms, the first being direct hydrophobic interaction of the lipid tail with a hydrophobic surface resulting in a monolayer of FSL at the surface. The second surface coating will be through the formation of bilayers, which probably either encapsulate fibres or being via the hydrophilic F group. This is the expected mechanism by which FSLs bind to fibrous membranes such as paper and glass fibres. A recent study has found that when FSL Kode constructs are optimised, could in a few seconds glycosylate almost any non-biological surface including metals, glass, plastics, rubbers, and other polymers.

LpxC contains a zinc-binding motif, which resides at the base of an active site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid. This tunnel accounts for the specificity of LpxC toward substrates and inhibitors bearing appropriately positioned 3-O-fatty acid substituents.

200x200px Influenza virus neuraminidase (vNEU) consists of 4 co-planar roughly spherical subunits predominantly made of β-sheets, characterized as a 6-fold β-propeller and a hydrophobic region embedded in the virus’ membrane.Colman, P.M. (1994) Influenza virus neuraminidase: Structure, antibodies, and inhibitors.Protein Science. 3: 1687–1696.

Acrylic MICS-IOL in holder The materials that have been used to manufacture intraocular lens implants include polymethylmethacrylate (PMMA), silicone, hydrophobic acrylate, hydrophilic acrylate and collamer.Belluci R. An Introduction to Intraocular Lenses: Material, Optics, Haptics, Design and Aberration. In: Güell JL (ed): Cataract. ESASO Course Series.

Maintaining a clean diamond can sometimes be difficult as jewelry settings can obstruct cleaning, and oils, grease, and other hydrophobic materials adhere well to a diamond. Many jewelers use steam cleaners. Some jewelers provide their customers with ammonia-based cleaning kits; ultrasonic cleaners are also popular.

Water-resistant mascaras require hydrophobic ingredients, like dodecane. Non water-resistant mascaras have base ingredients that are water-soluble. Mascaras designed to lengthen or curl the eyelashes often contain nylon or rayon microfibers. Additionally, ceresin, gum tragacanth, and methyl cellulose are regular ingredients and serve as stiffeners.

The oligomeric nature of the enzyme does not contribute to enzymatic activity, but serves to increase thermal stability through hydrophobic interactions and hydrogen bonding between interfacial residues. As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .

Froth flotation is one of the processes used to recover recycled paper. In the paper industry this step is called deinking or just flotation. The target is to release and remove the hydrophobic contaminants from the recycled paper. The contaminants are mostly printing ink and stickies.

Melittin produced a different conformational change than mastoparan. In an aqueous solution, melittin went from a nonhelical form to an alpha helix when phosphate was added to the solution. The binding of melittin to the membrane was believed to result from electrostatic interactions, not hydrophobic interactions.

PNIPA have been used in gel actuators, which convert external stimuli into mechanical motion. Upon heating above the LCST, the hydrogel goes from hydrophilic to hydrophobic state. This conversion results in an expulsion of water which causes a physical conformational change, creating a mechanical hinge movement.

MP196 is a synthetic antimicrobial peptide. It falls under the structural class: short cationic peptides. Since it is a short cationic peptide, it can be easily synthesized, derivatized and isolated. MP196 is rich in tryptophan, a hydrophobic amino acid and arginine residues, a positively charged amino acid.

RHCG plays a critical role in ammonium handling and pH homeostasis in the kidney. The structure of the RHCG protein; indicates that it has a hydrophobic ammonia-conducting channel and shows that it shares a common fold with the ammonia transporters, thus making it an ammonia transporter.

Env is generated by splicing and overlaps pol at the start. It encodes surface and transmembrane envelope proteins by being cleaved twice, a polypeptide precursor, and a hydrophobic region. Env plays a large role in the functionality of ENTV. Env is important in ENVT tissue selectivity.

It has been suggested that these two modules form a single structural and functional unit. The two domains keep their specific tertiary structure, but interact intimately to bury a hydrophobic core; the inter-module linker makes up the third strand of the EGF-module's major beta-sheet.

Emulsifiers produced by microbes can break up oil into smaller droplets, effectively increasing the available surface area. (2) Increase the bioavailability of hydrophobic water- insoluble substrates. Biosurfactants can enhance the availability of bound substrates by desorbing them from surfaces (e.g. soil) or by increasing their apparent solubility.

It is prepared by hydrothermal reaction using tetrapropylammonium hydroxide followed by calcining to remove residual ammonium salts. The compound is notable in being ca. 33% porous. It is useful because the material contains (SiO)10 rings that allow sorption of hydrophobic molecules of diameter 0.6 nm.

TMEM151A has no known isoforms, and is a part of family pfam15857 with one paralogue: TMEM151B. Tertiary structure TMEM151A as predicted by Swiss Model. The arrows represent beta sheets and the coils represent alpha helices. Predicted tertiary structure of TMEM151A with hydrophobic elements highlighted in green.

Poly(methyl acrylate) (PMA) is a hydrophobic synthetic acrylate polymer. PMA, though softer than polymethyl methacrylate (PMMA), is tough, leathery, and flexible. It has a low glass-transition temperature about 10°C (12.5°C in case of PMA38). High-energy radiation leads to cross linking in PMA.

New silicone- based compounds, such as polydimethylsiloxane, work by lubricating the fibers. Manufacturers use derivatives with amine- or amide-containing functional groups as well. These groups improve the softener's binding to fabrics. As softeners are often hydrophobic, they commonly occur in the form of an emulsion.

In the early formulations, manufactures used soaps as emulsifiers. The emulsions are usually opaque, milky fluids. However, there are also microemulsions, where the droplets of the hydrophobic phase are substantially smaller. Microemulsions provide the advantage of increased ability of smaller particles to penetrate into the fibers.

Farnesol is a natural 15-carbon organic compound which is an acyclic sesquiterpene alcohol. Under standard conditions, it is a colorless liquid. It is hydrophobic, and thus insoluble in water, but miscible with oils. Farnesol is produced from 5-carbon isoprene compounds in both plants and animals.

These pigments are in contact with a number of non- polar, hydrophobic residues. BChl a molecules that absorb at 800 nm are present in a relatively polar environment. The formulated N-terminus of the alpha polypeptide, a nearby histidine, and a water molecule are responsible for this.

Semple, K. T., Morris, A. W. J., & Paton, G. I. 2003. Bioavailability of hydrophobic organic contaminants in soils: fundamental concepts and techniques for analysis. European journal of soil science, 54(4), 809-818. Ionic compounds, such as heavy metals, can be precipitated into the solid phase.

Methanophenazine, a phenazine derivative, is a strongly hydrophobic redox- active cofactor with a role in electron transport in some methanogens. This chromophore can be purified from membranes of methanogenic archaea such as Methanosarcina mazei. The enzyme methanosarcina-phenazine hydrogenase (EC 1.12.98.3) has the name methanophenazine hydrogenase as a synonym.

Disperse Yellow 42 is one of the more common disperse dyes. Disperse dyes are dyes intended for polyester, acetate, and related hydrophobic fibers. It is estimated that 85% of disperse dyes are azos or anthraquinone dyes. Disperse dye have low solubility in water, typically less than 1 mg/L.

To enhance cleaning power, small amounts of detergent (0.5–1.5%) are added to the working solvent and are essential to its functionality. These detergents emulsify hydrophobic soils and keep soil from redepositing on garments. Depending on the machine's design, either an anionic or a cationic detergent is used.

PP1 works by using two manganese ions as catalysts for the dephosphorylation (see below). Surrounding these ions is a Y-shaped cleft with three grooves: a hydrophobic, an acidic, and a C-terminal groove. When PP1 is not bonded to any other subunit, it is not particularly specific.

Torrefaction also converts the biomass from a hydrophilic (water absorbing) to a hydrophobic (water repelling) state. Water repelling briquettes can be transported and stored outside, which simplifies the logistics operation and decreases cost. All biological activity is stopped, reducing the risk of fire and stopping biological decomposition like rotting.

More testing is needed to evaluate the performance of different implicit solvation models and parameter sets. They are often tested only for a small set of molecules with very simple structure, such as hydrophobic and amphiphilic alpha helixes (α). This method was rarely tested for hundreds of protein structures.

Compared to the reference set of human proteins, TMED5 has fewer alanine and proline residues but more aspartic acid and phenylalanine residues.European Molecular Biology Laboratory - European Bioinformatics Institute (EMBL-EBI). "Statistical Analysis of Protein Sequences (SAPS)". TMED5 isoform 1 has one hydrophobic segment that corresponds with its transmembrane region.

These coatings are usually based on organic polymers, which allow researchers to add additional functions, such as antimicrobial activity. There are two classes of non-toxic anti-fouling coatings. The most common class relies on low friction and low surface energies. Low surface energies result in hydrophobic surfaces.

Graphene oxide flakes in polymers display enhanced photo-conducting properties. Graphene is normally hydrophobic and impermeable to all gases and liquids (vacuum-tight). However, when formed into graphene oxide-based capillary membrane, both liquid water and water vapor flow through as quickly as if the membrane was not present.

Although it is somewhat hydrophobic, phosgene reacts with water to release hydrogen chloride and carbon dioxide: :COCl2 \+ H2O → CO2 \+ 2 HCl Analogously, with ammonia, one obtains urea: :COCl2 \+ 4 NH3 → CO(NH2)2 \+ 2 NH4Cl Halide exchange with nitrogen trifluoride and aluminium tribromide gives COF2 and COBr2, respectively.

Replacing the conserved glycine with L-alanine resulted in subtle VCC differences. Comprehensive alanine scanning mutagenesis of HNP1 and HD5 demonstrated the importance of bulky hydrophobic residues. These studies have recently been expanded to include additional beta defensins, theta defensins, and the human cathelicidin LL-37 and related peptides.

TMEM33 has a significantly high net positive charge and quantity of hydrophobic residues. In particular, leucine that makes up 17.8% of the human TMEM33 protein. TMEM33 contains a conserved domain in the protein super family UPF0121, in Homo sapiens this region spans from amino acids 1 to 246.

ADP binds behind the NAD-BD, just beneath the pivot helix - the second coenzyme binding site. The adenosine moiety binds down into a hydrophobic pocket with the ribose phosphate groups pointing up toward the pivot helix. ADP can also bind to the second, inhibitory, NADH-site yet causes activation.

Siloxane is known to be hydrophobic. Noted for large molecular structure, siloxane is frequently used for sealing exterior concrete, porous concrete block and porous brick. Siloxane is generally applied only to fully cured existing concrete. In summary, all major concrete sealer chemistries can have valuable and practical applications.

The active site has been found to be suboptimally hydrated, resulting in ligand binding being driven by enthalpic dispersion forces. This is contrary to most other proteins, which exhibit entropy-driven binding forces from the reorganisation of water molecules. This unusual process has been termed the nonclassical hydrophobic effect.

Thus, the higher redox potentials have been attributed to the exclusion of water from the metal-binding site, a condition augmented by the presence of bulky hydrophobic residues. Conversely, negatively charged residues lower the redox potential, since they stabilize the more positively charged cupric form of the copper ion.

Also in this paper she reports values of the thickness of films of various amphiphillic substances on the surface of water.Pockels, A. (1892). Nature, 46, 418. In a later paper Pockels examined the effects of different ratios of hydrophobic to amphiphilic molecules on surface tension and monolayer formation.

One important application are the many macrocyclic antibiotics, the macrolides, e.g. clarithromycin. Many metallocofactors are bound to macrocyclic ligands, which include porphyrins, corrins, and chlorins. These rings arise from multistep biosynthetic processes that also feature macrocycles. Macrocycles often bind ions and facilitate ion transport across hydrophobic membranes and solvents.

To prevent snow from balling up under crampons, especially in temperatures around freezing, most models can be fitted with plastic or rubber "anti-balling" systems to reduce build-up. Rubber models use flexion to repel snow while plastic anti-balling plates employ a hydrophobic surface to prevent adhesion.

Assembly of the hydrophobic anchor consisting of subunits SDHC and SDHD remains unclear. Especially in case of heme b insertion and even its function. Heme b prosthetic group does not appear to be part of electron transporting pathway within the complex II. The cofactor rather maintains the anchor stability.

This makes the environment around the chromophore in mCherry more hydrophobic than the environment around the chromophore of DsRed. The end termini on mCherry are GFP-like which allows it to be incorporated in to systems where GFP can be used and mRFP1 could not have been used.

Most nonpolar molecules are water-insoluble (hydrophobic) at room temperature. Many nonpolar organic solvents, such as turpentine, are able to dissolve non-polar substances. In the methane molecule (CH4) the four C−H bonds are arranged tetrahedrally around the carbon atom. Each bond has polarity (though not very strong).

Salts of naphthenic acids, called naphthenates, are widely used as hydrophobic sources of metal ions in diverse applications.[2]Aluminium salts of naphthenic acid and palmitic acid were combined during World War II to produce napalm. The word "napalm" is derived from the words naphthenic acid and palmitic acid.

Silicone-based defoamers are polymers with silicon backbones. These might be delivered as an oil or a water based emulsion. The silicone compound consists of a hydrophobic silica dispersed in a silicone oil. Emulsifiers are added to ensure that the silicone spreads fast and well in the foaming medium.

This conformational change is different from most EF hands, in that the entering helix, and not the exiting helix, moves. This conformational change exposes a large hydrophobic pocket between helix 3, 4, and the hinge region of S100A1 that is involved in virtually all calcium-dependent target protein interactions.

Schematic representation of the different types of interaction between monotopic membrane proteins and the cell membrane: 1. interaction by an amphipathic α-helix parallel to the membrane plane (in-plane membrane helix) 2. interaction by a hydrophobic loop 3. interaction by a covalently bound membrane lipid (lipidation) 4.

Various selective DRIs are known, in contrast to the case of DRAs. It is particularly of note that the mechanism of action at the dopamine transporter (DAT) for dopamine releasers/substrates is entropy-driven (i.e. hydrophobic), whereas for dopamine re-uptake inhibitors it is enthalpy-driven (i.e. conformational change).

The majority of the residues coming from the β sheet are hydrophobic with Asp449 being the exception. This residue is invariant and forms a hydrogen bond along with a water molecule to the adenine amine group. Three other water molecules form direct hydrogen bonds with the adenine base.

A hydrophobic portion of III inserts itself into the inner membrane, fastening the phage particle to the host and distributing the coat proteins into the host membrane. It is the degradation of the major coat protein that causes the genome to be released into the cytoplasm of the host.

The best known sterol is cholesterol, which is found in humans. Cholesterol also occurs naturally in other eukaryote cell membranes. Sterols have a hydrophobic four-membered fused ring rigid structure, and a small polar head group. Cholesterol is bio-synthesised from mevalonate via a squalene cyclisation of terpenoids.

A test of super- hydrophobic paint. Active recent research on superhydrophobic materials might eventually lead to industrial applications. Some attempts at fabricating a superhydrophobic surface include mimicking a lotus leaf surface, namely the two-tiered characteristic. This requires micro-scale surfaces with typically nanoscale features on top of them.

Solvent often influences folding. For example, a folding pathway involving hydrophobic collapse would fold differently in a nonpolar solvent. This difference is due to the fact that different solvents stabilize different intermediates of the folding pathway as well as different final foldamer structures based on intermolecular noncovalent interactions.

In molecular biology, the protein domain TyeA is short for Translocation of Yops into eukaryotic cells A. It controls the release of Yersinia outer proteins (Yops) which help Yersinia evade the immune system. More specifically, it interacts with the bacterial protein YopN via hydrophobic residues located on the helices.

The role of glide wax is to adapt and improve the friction properties of a ski base to the expected snow properties to be encountered on a spectrum from cold crystalline snow to saturated granular snow. Modern ski bases often are made from ultra-high- molecular-weight polyethylene (UHMWPE). Kuzmin asserts that UHMWPE is non- porous and can hold neither wax nor water, so there is no possibility for filling pores; furthermore, he asserts that UHMWPE is very hydrophobic, which means that wet snow does not appreciably retard the ski and that glide wax offers little additional ability to repel water. He notes that clear bases are more durable and hydrophobic than those with carbon content.

The organisation of large proteins by structural domains represents an advantage for protein folding, with each domain being able to individually fold, accelerating the folding process and reducing a potentially large combination of residue interactions. Furthermore, given the observed random distribution of hydrophobic residues in proteins, domain formation appears to be the optimal solution for a large protein to bury its hydrophobic residues while keeping the hydrophilic residues at the surface. However, the role of inter- domain interactions in protein folding and in energetics of stabilisation of the native structure, probably differs for each protein. In T4 lysozyme, the influence of one domain on the other is so strong that the entire molecule is resistant to proteolytic cleavage.

Surfactant–like peptides which undergo self-assembly in water to form nanotubes and nanovesicles have been designed using natural lipids as a guide. This class of peptides has a hydrophilic head (with one or two charged amino acids such as aspartic and glutamic acids, or lysine or histidine acids) with a hydrophobic tail (with 4 or more hydrophobic amino acids such as alanine, valine or leucine). The peptide monomers are about 2-3 nm long and consist of seven or eight amino acids; the length of the peptide can be adjusted by adding or removing acids. FIGURE 3: NATURAL AMINO ACIDS USED IN THE DESIGNER SUFACTANT PEPTIDES FIGURE 4: MOLECULAR MODELS OF SOME SURFACTANT PEPTIDES.

His lab is devoted towards synthesizing hydrophobic surfaces, diamond stationary phases for liquid chromatography and microfabricated TLC plates. Lindford works in surface modification and characterization, particularly in studying organic thin films (monolayer and polymer), modifying silicon, diamond, silicon oxide, gold, and polymers, surface patterning, surface organic chemistry, thin-film deposition with silanes, alkenes, thiols, and by sputtering. In his group they also undertake liquid chromatography (HPLC and TLC) and solid phase extraction (SPE), develop hydrophobic coatings for various materials, study materials for optical data storage, and perform surface analysis by XPS, ToF-SIMS, wetting, optical ellipsometry, and FTIR. His lab also performs chemometrics of mass spec data (PCA, MCR, cluster analysis, and PLS).

The BAX gene was the first identified pro-apoptotic member of the Bcl-2 protein family. Bcl-2 family members share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4), and can form hetero- or homodimers. These domains are composed of nine α-helices, with a hydrophobic α-helix core surrounded by amphipathic helices and a transmembrane C-terminal α-helix anchored to the mitochondrial outer membrane (MOM). A hydrophobic groove formed along the C-terminal of α2 to the N-terminal of α5, and some residues from α8, binds the BH3 domain of other BAX or BCL-2 proteins in its active form.

This is a critical modification for plasma membrane targeting. In the membrane-unbound form, the MA myristoyl fatty acid tail is sequestered in a hydrophobic pocket in the core of the MA protein. Recognition of plasma membrane PI(4,5)P2 by the MA HBR activates the "myristoyl switch", wherein the myristoyl group is extruded from its hydrophobic pocket in MA and embedded in the plasma membrane. In parallel to (or possibly concomitant with) myristoyl switch activation, the arachidonic acid moiety of PI(4,5)P2 is extracted from the plasma membrane and binds in a channel on the surface of MA (which is distinct from that previously occupied by the MA myristoyl group.

Based on crystallographic studies conducted with recombinant extracellular mouse JAMs (rsJAM) and human JAMs (hJAM), it has been shown that JAM consists of immunoglobulin-like V-set domain followed by a second immunoglobulin domain that are linked together by a short linker sequence. The linker makes extensive hydrogen bonds to both domains, and the side chain of one of the main linker residues, Leu128, is commonly embedded in a hydrophobic cleft between each immunoglobulin-like domain. Two JAM molecules contain N-terminal domains that react in a highly complementary fashion due to prolific ionic and hydrophobic interactions. These two molecules form U-shaped dimers and salt bridges are then formed by a R(V,I,L)E motif.

The critical role of the intimate relationship between the hydrophobic side chain of raloxifene and the hydrophobic residue of the receptor to change both the shape and charge of the external surface of a SERM-ER complex has been confirmed with raloxifene derivatives. When the interactive distance between raloxifene and Asp-351 is increased from 2.7 Å to 3.5-5 Å it causes increased estrogen-like action of the raloxifene-ERα complex. When the piperidine ring of raloxifene is replaced by cyclohexane, the ligand loses antiestrogenic properties and becomes a full agonist. The interaction between SERM's antiestrogenic side chain and amino acid Asp-351 is the important first step in silencing AF-2.

An ATPase (NSF) together with a cofactor (α-SNAP) facilitates the breakdown of the SNARE complex after the completion of exocytosis. Studies have suggested that, during the disassociation process, the NSF/α-SNAP complex acts specifically on the zero ionic layer, particularly, the glutamine residue (Q226) in Syntaxin. The glutamine residue transmits the conformational change of NSF/α-SNAP complex to the SNARE complex in order to disrupt and thus disassociate the SNARE complex at the zero ionic layer. More specifically, even though the ionic layer is buried within the hydrophobic complex for the most part, during disassociation, NSF/α-SNAP complex may disturb the hydrophobic shielding and thus let water molecules into the core.

Moving outwards away from the hydrophobic core region and into the interfacial hydrophilic region, the effective concentration of water rapidly changes across this boundary layer, from nearly zero to a concentration of around 2 M. The phosphate groups within phospholipid bilayers are fully hydrated or saturated with water and are situated around 5 Å outside the boundary of the hydrophobic core region (see Figures ). Some water-soluble proteins associate with lipid bilayers irreversibly and can form transmembrane alpha-helical or beta-barrel channels. Such transformations occur in pore forming toxins such as colicin A, alpha-hemolysin, and others. They may also occur in BcL-2 like protein , in some amphiphilic antimicrobial peptides , and in certain annexins .

A chromatogram of complex mixture (perfume water) obtained by reversed phase HPLC Reversed phase HPLC (RP-HPLC) has a non-polar stationary phase and an aqueous, moderately polar mobile phase. One common stationary phase is a silica which has been surface-modified with RMe2SiCl, where R is a straight chain alkyl group such as C18H37 or C8H17. With such stationary phases, retention time is longer for molecules which are less polar, while polar molecules elute more readily (early in the analysis). An investigator can increase retention times by adding more water to the mobile phase; thereby making the affinity of the hydrophobic analyte for the hydrophobic stationary phase stronger relative to the now more hydrophilic mobile phase.

The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute forming a clathrate-like structure around the non-polar molecules. This structure formed is more highly ordered than free water molecules due to the water molecules arranging themselves to interact as much as possible with themselves, and thus results in a higher entropic state which causes non-polar molecules to clump together to reduce the surface area exposed to water and decrease the entropy of the system. Thus, the two immiscible phases (hydrophilic vs. hydrophobic) will change so that their corresponding interfacial area will be minimal.

Tetrahedron Lett. 33, 5791^5794 the cyclopentane derivatives was designed with a guanidino group replacing C4-hydroxyl position of DANA in the active site, similar to Zanamivir. Babu et al. found that the addition of n-butyl side chain makes the compound fit better to the hydrophobic region of the enzyme.

Limnodrilus hoffmeisteri is well recognized indicator of organic pollution and low dissolved oxygen. It is increasingly being used to test the toxicity of sediment-associated contaminants and their bioaccumulation. Recent study demonstrated that Limnodrilus hoffmeisteri can bioaccumulate hydrophobic contaminants and even degrade them depending on the structure and properties of contaminants.

Vibriolysin (, Aeromonas proteolytica neutral proteinase, aeromonolysin) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin This thermostable enzyme is isolated from Vibrio proteolyticus.

However, it was discovered afterwards that secondary interactions can be applied for improving separation power. In 1986, Regnier’s group synthesized a stationary phase that had characteristics of anion exchange chromatography (AEX) and hydrophobic interaction chromatography (HIC) on protein separation. L.A. Kennedy, W. Kopaciewicz, F.E. Regnier, J. Chromatogr. 359 (1986) 73.

Arenicin-3 is a 21 amino acid peptide with the sequence GFCWYVCYRNGVRVCYRRCN. It has two disulfide bonds bridging between Cys2, Cys20 and Cys7, Cys16. In aqueous solution arenicin-3 takes on a beta hairpin structure. Due to the 4 positive arginines along with nine hydrophobic amino acids, arenicin-3 is amphipathic.

Mulches, erosion cloth and seeding retard overland flow and protect soil from rain drop impact and increase soil moisture holding capacity. Landscape structures (e.g., log erosion barriers, contour trenches, straw wattles) trap sediment and prevent slope rilling. Strip tillage and chemicals break up or reduce hydrophobic soils and improve infiltration.

Molecular surface of the CT active site, showing a deep canyon where both substrates are bound. (d). Schematic drawing of the CT active site. The biotin-binding pocket of PCC is hydrophobic and highly conserved. Biotin and propionyl-CoA bind perpendicular to each other in the oxyanion hole-containing active site.

The protein is a nuclear encoding mitochondrial protein. The protein in humans has 1760 amino acids. The protein is considered largely neutral, though 17% of the primary structure is composed of the hydrophobic leucine-rich repeats. The leucine-rich repeat forms a structural horseshoe shape, which encourages protein-protein interactions.

An effect similar to coaxial stacking has been observed in rationally designed DNA structures. DNA origami structures contain a large number of double helixes with exposed blunt ends. These structures were observed to stick together along the edges that contained these exposed blunt ends, due to the hydrophobic stacking interactions.

Another type of drug delivery vehicle used is polymeric micelles. They are prepared from certain amphiphilic co-polymers consisting of both hydrophilic and hydrophobic monomer units. They can be used to carry drugs that have poor solubility. This method offers little in the terms of size control or function malleability.

A ligand-gated channel requires a chemical, such as a neurotransmitter, to activate the channel. Stress-gated channels require a mechanical force applied to the channel for opening. Aquaporins are dedicated channels for the movement of water across the hydrophobic interior of the cell membrane.Verkman, A. (2011) Aquaporins at a Glance.

The most work investigating crystalline structures have been done on PorA and PorB of Zobellia galactinovirans. The L6S unit at subsite −2 is surrounded by tryptophan and arginine residues in both PorA and PorB, which construct a positively charged hydrophobic pocket that allows for a bulky sulfate group to fit.

The requirements for a self-cleaning hydrophobic surface are a very high static water contact angle θ, the condition often quoted is θ>160°, and a very low roll-off angle, i.e. the minimum inclination angle necessary for a droplet to roll off the surface.Marmur, A. Langmuir 20, 3517–3519, (2004).

The secondary structures are tightly packed in the protein core in a hydrophobic environment. Each amino acid side group has a limited volume to occupy and a limited number of possible interactions with other nearby side chains, a situation that must be taken into account in molecular modeling and alignments.

Furthermore, the solubility in water plays a significant role in the effectiveness of biotransformation in an environment. The butyl group gives BBP a slightly more hydrophobic property, compared to other plasticizer it is relatively good soluble. The longer the alkyl chain the less soluble and the less well it is degenerated.

For gamma(γ)-tocopherol: R1 = H, R2 = methyl group, R3 = methyl group. For delta(δ)-tocopherol: R1 = H, R2 = H, R3 = methyl group. The same configurations exist for the tocotrienols, except that the hydrophobic side chain has three carbon-carbon double bonds whereas the tocopherols have a saturated side chain.

It is one of several organic volatiles produced by the Arabidopsis lyrata ssp. petraea flower in response to insect feeding. Because of its hydrophobic nature, nerolidol is easily permeable across the plasma membrane and can interact with intracellular proteins. However it has a high cytotoxic potential and can disrupt the membrane.

Informations for this group of inhibitors are quite restricted. Azetidine-based DPP-4 inhibitors can roughly be grouped into three main subcategories: 2-cyanoazetidines, 3-fluoroazetidines, and 2-ketoazetidines. The most potent ketoazetidines and cyanoazetidines have large hydrophobic amino acid groups bound to the azetidine nitrogen and are active below 100nM.

Early cotton softeners were typically based on a water emulsion of soap and olive oil, corn oil, or tallow oil. Softening compounds differ in affinity to various fabrics. Some work better on cellulose-based fibers (i.e., cotton), others have higher affinity to hydrophobic materials like nylon, polyethylene terephthalate, polyacrylonitrile, etc.

Recent data suggest hydrophobic interactions could be the main contributor. It is difficult to discern the exact mechanism of binding because of the complex water-ice interface. Currently, attempts to uncover the precise mechanism are being made through use of molecular modelling programs (molecular dynamics or the Monte Carlo method).

Reticulons do not have an ER localization sequence, but the RHD hydrophobic region is able to target protein-RTN to the ER by green fluorescence. Without the RHD, there is no association with the ER. Reticulons have localized to the ER in the following organisms: yeast, Arabidopsis, Xenopus, Drosophilia and mammals.

Conversely, an antichaotropic agent (kosmotropic) is a molecule in an aqueous solution that will increase the hydrophobic effects within the solution. Antichaotropic salts such as ammonium sulphate can be used to precipitate substances from the impure mixture. This is used in protein purification processes, to remove undesired proteins from solution.

Such interactions are subject to steric effects in that very large molecules may have only restricted access to the pores of the stationary phase, where the interactions with surface ligands (alkyl chains) take place. Such surface hindrance typically results in less retention. Retention time increases with hydrophobic (non-polar) surface area.

It has been suggested, through evidence provided by contour maps of water density, that the interior of XPO5 is hydrophilic, while the exterior of XPO5 is hydrophobic. Therefore, this enhances the binding capabilities of XPO5 to the nuclear pore complex, allowing for transport of the ternary complex out of the nucleus.

The substrate must bind near the active site in order for the reaction to take place. Near to the iron centers, there are hydrophobic pockets. It is thought that here the methane binds and is held until needed. From the X-ray crystallography, there is no direct path to these packets.

Primary sequence of SMIM15 is: MFDIKAWAEY VVEWAAKDPY GFLTTVILAL TPLFLASAVL SWKLAKMIEA REKEQKKKQK. RQENIAKAKR LKKD Molecular weight of SMIM15 has been found to be 8.6 kdal and it has a pI of 9.82. There are no significant compositional features compositional features like charge clusters, hydrophobic segments, charge runs, patterns, multiplets or periodicities.

Rhizopuspepsin (, Rhizopus aspartic proteinase, neurase, Rhizopus acid protease, Rhizopus acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. From the zygomycete fungus Rhizopus chinensis.

A SAPS analysis on the human CDV3 protein sequence found one uncharged cluster segment from 28-75 aa. There were no signs of high scoring hydrophobic segments. One high scoring transmembrane segment was found from 28-55 aa. CDV3 was found to have significant maximal spacing from 27-76 aa.

The C-terminal domain makes numerous electrostatic interactions with an anion-binding exosite of thrombin, while the last five residues are in a helical loop that forms many hydrophobic contacts. Natural hirudin contains a mixture of various isoforms of the protein. However, recombinant techniques can be used to produce homogeneous preparations of hirudin.

Highly hydrophobic surfaces made of low surface energy (e.g. fluorinated) materials may have water contact angles as high as ≈ 120°. Some materials with highly rough surfaces may have a water contact angle even greater than 150°, due to the presence of air pockets under the liquid drop. These are called superhydrophobic surfaces.

In 2013, P2i diversified its marketing, replacing Aridion with the term Splash-proof, to identify the traditional hydrophobic layer technology. P2i has partnered with Motorola and Huawei and several other top smartphone brands, as well as another leading Chinese manufacturers. P2i has the capability to treat over half a billion phones in 2019.

Chemically they have a prenyl group attached to their flavonoid backbone. It is usually assumed that the addition of hydrophobic prenyl groups facilitate attachment to cell membranes. Prenylation may increase the potential activity of its original flavonoid. Monoprenyl isoflavone epoxidase is a key enzyme in fungal Botrytis cinerea metabolism of prenylated flavonoids.

When lyophilic sols are added to lyophobic sols, depending on their sizes, either lyophobic sol is adsorbed in the surface of lyophilic sol or lyophilic sol is adsorbed on the surface of lyophobic sol. The layer of the protective colloid prevents direct collision between the hydrophobic colloidal particles and thus prevents coagulation.

Transmembrane domains are conserved in most orthologs, including all mammals. Relative to other proteins, TMEM8B has higher than normal levels of K, Lysine, and L, Leucine. There are three repeating leucine-rich regions within conserved domains of TMEM8B, all 4 amino acids long. Leucine rich regions can result in hydrophobic interactions within themselves.

Rhodococci also contain characteristics that enhances their ability to degrade organic pollutants. Their hydrophobic surface allows for adhesion to hydrocarbons, which enhances its ability to degrade these pollutants. They have a wide variety of catabolic pathways and many unique enzyme functions. This gives them the ability to degrade many recalcitrant, toxic hydrocarbons.

Sphingosine Glycosphingolipids are a subtype of glycolipids containing the amino alcohol sphingosine. They may be considered as sphingolipids with an attached carbohydrate. Glycosphingolipids are a group of lipids (more specifically, sphingolipids) and are a part of the cell membrane. They consist of a hydrophobic ceramide part and a glycosidically bound carbohydrate part.

Drugs diffuse through capillary walls in the same manner as endogenous molecules. One of the most important examples of this is drug diffusion across the blood brain barrier. The blood brain barrier consists of a bed of continuous capillaries. Typically only small hydrophobic molecules are able to diffuse across the blood brain barrier.

Both varieties of membrane are chosen for their non-specific protein binding properties (i.e. binds all proteins equally well). Protein binding is based upon hydrophobic interactions, as well as charged interactions between the membrane and protein. Nitrocellulose membranes are cheaper than PVDF, but are far more fragile and cannot withstand repeated probings.

Unlike the hydrophobic pocket and the positively charged exosite, the catalytic triad sequence is precisely conserved in both thrombins from different species andcerastocytin:Dekhil et al. (2003) Molecular Cloning and Expression of a Functional Snake Venom Serine Proteinase, with Platelet Aggregating Activity, from the Cerastes cerastes Viper. Biochemistry 42: 10609-10618. His57, Asp102, Ser195.

The utility of fluorous chemistry hinges on the partitioning modality distinct from polar/non-polar or hydrophilic/hydrophobic. A major application of fluorous chemistry involves the use of fluorosurfactant perfluorooctanoic acid (PFOA) to facilitate the production of Teflon. The technology is controversial because of the slow rates of biodegradation of such compounds.

Cytohesin-interacting protein is a protein that in humans is encoded by the CYTIP gene. The protein encoded by this gene contains 2 leucine zipper domains and a putative C-terminal nuclear targeting signal, and it does not have any hydrophobic regions. This protein is expressed weakly in resting NK and T cells.

Figure 4. The best fit mapped with the four features of the pharmacophore. In the drug discovery process of a 5-HT2C agonist, a pharmacophore module has been used to discover novel 5-HT2C receptor ligands. The pharmacophore has four features; one aromatic ring, two hydrophobic features and one positive ionizable feature.

When the IBD column compared to recently established PNIPAAm columns, electrostatic forces show remarkably higher retention ability of charged compounds than its hydrophilic predecessor. A single stationary phase can accomplish pharmaceutical separations based on hydrophobic interactions, hydrophilic interactions, and electrostatic interactions merely by adjusting the temperature (while adjusting pH to tweak the LCST).

Carvedilol is a basic, hydrophobic compound with a steady-state volume of distribution of 115 L. Plasma clearance ranges from 500 to 700 mL/min. Absorption is slowed when administered with food, however, it does not show a significant difference in bioavailability. Taking carvedilol with food decreases the risk of orthostatic hypotension.

The strong interaction between folic acid and folate receptor was attributed to both hydrogen bonds and hydrophobic interactions. The study of non-covalent interactions is also used to study binding and cooperativity in supramolecular assemblies and macrocyclic compounds such as crown ethers and cryptands, which can act as hosts to guest molecules.

Superhydrophobic or hydrophobic properties have been used in dew harvesting, or the funneling of water to a basin for use in irrigation. The Groasis Waterboxx has a lid with a microscopic pyramidal structure based on the ultrahydrophobic properties that funnel condensation and rainwater into a basin for release to a growing plant's roots.

A carbon–silicon bond present in all organosilicon compounds Organosilicon compounds are organometallic compounds containing carbon–silicon bonds. Organosilicon chemistry is the corresponding science of their preparation and properties. Most organosilicon compounds are similar to the ordinary organic compounds, being colourless, flammable, hydrophobic, and stable to air. Silicon carbide is an inorganic compound.

Pregnenolone is also known chemically as pregn-5-en-3β-ol-20-one. Like other steroids, it consists of four interconnected cyclic hydrocarbons. The compound contains ketone and hydroxyl functional groups, two methyl branches, and a double bond at C5, in the B cyclic hydrocarbon ring. Like many steroid hormones, it is hydrophobic.

The chloroplast NADH dehydrogenase F (ndhF) gene is found in all vascular plant divisions and is highly conserved. Its DNA fragment resides in the small single-copy region of the chloroplast genome, and is thought to encode a hydrophobic protein containing 664 amino acids and to have a mass of 72.9 kDa.

The light emitted from cavitation bubbles is termed sonoluminescence. Use of this technology has been tried successfully in alkali refining of vegetable oils. Hydrophobic chemicals are attracted underwater by cavitation as the pressure difference between the bubbles and the liquid water forces them to join together. This effect may assist in protein folding.

Surface modification makes paper hydrophobic and oleophilic. This combination allows ink oil to penetrate the paper, but prevents dampening water absorption, which increases papers printability. Three different plasma-solid interactions are used: etching/ablation, plasma activation, and plasma coating. Etching or ablation is when material is removed from the surface of the solid.

AKR1B1 consists of 316 amino acid residues and weighs 35853Da. It does not possess the traditional dinucleotide binding fold. The way it binds NADPH differs from other nucleotide adenine dinucleotide- dependent enzymes. The active site pocket of human aldose reductase is relatively hydrophobic, lined by seven aromatic and four other non-polar residues.

Only minor changes on the pyrrolidine ring can be tolerated, since the good fit of the ring with the hydrophobic S1 pocket is very important for high affinity. Some trials have been made, e.g. by replacing the pyrrolidine with a thiazoline. That led to improved potency but also loss of chemical stability.

Hydroxyethyl cellulose is a gelling and thickening agent derived from cellulose. It is widely used in cosmetics, cleaning solutions, and other household products. Hydroxyethyl cellulose and methyl cellulose are frequently used with hydrophobic drugs in capsule formulations, to improve the drugs' dissolution in the gastrointestinal fluids. This process is known as hydrophilization.

The enzyme substrate complex is maintained by several non-covalent interactions: hydrophobic and polar interactions. The process is limited by the peptide size. Thus, only peptides with approximately the same volume (∼3,000 Å3) can be degraded by the enzyme. Peptides that can be cleaved off are between 8 and 23 amino-acid residues.

The polar part of xanthate molecule attaches to the ore particles with the non-polar hydrocarbon part sticking out and forming a hydrophobic layer. Then the particles are brought to the water surface by air bubbles. Only a small amount of about 300 g/tonne of ore is required for efficient separation.

These proteins are 190-240 amino acyl residues in length and possess six hydrophobic regions. PhoA fusion analyses of LysE of C. glutamicum provided evidence for a 5 transmembrane α-helical spanner (TMS) typology with the N-terminus inside and the C-terminus outside. However, some evidence suggests a 6 TMS topology.

The discovery of the hydrophobic pocket capable of binding ethanol is significant in the field of clinical pharmacology. Agents that can act as agonists to this binding site can be potentially useful in the creation of drugs for the treatment of neurological disorders such as epilepsy in which neuronal firing exceeds normal levels.

AKD's feature hydrophobic alkyl groups extending from a beta-propiolactone ring. A specific example is derived from the dimerization of the ketene of stearic acid. This ketene is generated by pyrolysis of stearoyl chloride.Raimund Miller, Claudio Abaecherli, Adel Said, Barry Jackson "Ketenes" in Ullmann's Encyclopedia of Industrial Chemistry, 2001, Wiley-VCH, Weinheim.

Specificity is endowed by the large contact area between enzyme and substrate. Proteases such as trypsin have specificity for one residue before and after the cleaved bond due to a shallow binding cleft with only one or two pockets that bind the substrate side chains. Conversely, viral proteases such as TEV protease have a long C-terminal tail which completely covers the substrate to create a binding tunnel. This tunnel contains a set of tight binding pockets such that each side chain of the substrate peptide (P6 to P1’) is bound in a complementary site (S6 to S1’). In particular, peptide side chain P6-Glu contacts a network of three hydrogen bonds; P5-Asn points into the solvent, making no specific interactions (hence the absence of substrate consensus at this position); P4-Leu is buried in a hydrophobic pocket; P3-Tyr is held in a hydrophobic pocket with a short hydrogen bond at the end; P2-Phe is also surrounded by hydrophobes including the face of the triad histidine; P1-Gln forms four hydrogen bonds; and P1’-Ser is only partly enclosed in a shallow hydrophobic groove.

Hsp90, while in the open conformation, leaves some hydrophobic residues exposed, to which unfolded and misfolded proteins that have unusual hydrophobic regions exposed are recruited with high affinity. When a bound substrate is in place, the energy-releasing ATP hydrolysis by the ATPase function near the N-terminal domain forces conformational changes that clamp the Hsp90 down onto the substrate. In a reaction similar to that of other molecular clamp proteins like GyrB and MutL, this site drives virtually all of the protein folding functions that Hsp90 plays a role in. In contrast, MutL and GyrB function as topoisomerases and use a charge clamp with a high amount of positively charged sidechains that is electrostatically attracted to the negative backbone of DNA.

This distorted structure forms a sialosyl cation after the release of the aglycon and is then trapped in the active site by a nucleophilic attack of the tyrosine residue. The orientation of the substrate in the active site is facilitated mainly by three strain-preserved Arginine residues binding the C1 acid group with salt bridges. Furthermore, the active site consists of eight other highly conserved amino acid-residues that make direct contact to the substrate or its derivatives. Including a glutamic acid residue binding the C7 and C9 alcohol groups on the glycerol side-chain (at C6) with hydrogen bonds and several hydrophobic residues correlating with the methyl group on the C5 N-acetyl and the hydrophobic backbone of the glycerol.

Seong and Matzinger have suggested that the "patterns" that the immune system recognizes on bacteria are not as different from the alarm signals released by damaged cells as one might have thought. They suggested that, because life evolved in water, the hydrophobic portions of molecules are normally hidden in the internal parts of molecules or other structures (like membranes) and that the sudden exposure of a hydrophobic portion is a sure sign that some injury or damage has occurred. They suggested that these are the most ancient alarm signals, that they are recognized by evolutionarily ancient systems of repair and remodeling, and that the modern immune system piggy-backed on this ancient system. Thus bacteria and other organisms may have very similar alarm systems.

The enzymatic structure of the human cholesterol-24 hydroxylase was determined via crystallography at the Stanford Synchrotron Radiation Lightsource, and was shown to be a 57kDa (500 residue) monomeric heme-containing protein bound to the endoplasmic reticulum in neurons. Cholesterol-24 hydroxylase active site and heme molecule with bound cholesterol 3-sulfate. Hydrophobic residues interacting with the aliphatic tail of the cholesterol are labelled in white. Created in pyMOL from PDB 2Q9F Cholesterol-24 hydroxylase is similar in structure to many other cytochrome P450s, possessing, for example, the conserved stretch of 23 hydrophobic residues in the N-terminus that make up a transmembrane-anchoring domain (residues 3-27). Cholester-24 hydroxylase (CYP46A1) with placement of active site shown in red.

The amino acids that make up a particular helix can be plotted on a helical wheel, a representation that illustrates the orientations of the constituent amino acids (see the article for leucine zipper for such a diagram). Often in globular proteins, as well as in specialized structures such as coiled-coils and leucine zippers, an α-helix will exhibit two "faces" one containing predominantly hydrophobic amino acids oriented toward the interior of the protein, in the hydrophobic core, and one containing predominantly polar amino acids oriented toward the solvent-exposed surface of the protein. Changes in binding orientation also occur for facially-organized oligopeptides. This pattern is especially common in antimicrobial peptides, and many models have been devised to describe how this relates to their function.

In the translation of messenger RNA molecules to produce polypeptides, cysteine is coded for by the UGU and UGC codons. Cysteine has traditionally been considered to be a hydrophilic amino acid, based largely on the chemical parallel between its sulfhydryl group and the hydroxyl groups in the side chains of other polar amino acids. However, the cysteine side chain has been shown to stabilize hydrophobic interactions in micelles to a greater degree than the side chain in the nonpolar amino acid glycine and the polar amino acid serine. In a statistical analysis of the frequency with which amino acids appear in different chemical environments in the structures of proteins, free cysteine residues were found to associate with hydrophobic regions of proteins.

In many current biofuel generation endeavours, the processes of differentiating and separating desired components from undesired ones leads to losses in both net energy yield and capital loss. Due to this, LS9 has developed a process where in their reaction chambers, shown above, utilize the natural properties of their desired components. Using both solvent composition and the realization that most desired components in biofuel generation possess a certain degree of hydrophobicity, LS9 has engineered their microbes to carry out their reactions in the aqueous-like phase, which is of lower hydrophobic character, and their desired components are secreted and float to the top forming a hydrophobic phase. This phase is easily accessible to collection apparatuses and requires little energy to collect.

Microtubules are composed of tubulin protein dimer subunits. The dimers each have hydrophobic pockets that are 8 nm apart and may contain delocalized pi electrons. Tubulins have other smaller non-polar regions that contain pi electron-rich indole rings separated by about 2 nm. Hameroff proposed that these electrons are close enough to become entangled.

Supporting evidence comes from that mutation of this tryptophan residue leads to a lower stability of the active form of galactose oxidase. Additionally, the outer sphere of the active site consists of many aromatic residues that give the active site a hydrophobic character. There are also extensive hydrogen bonding networks surround the active site.

The most common transcript encodes a protein that is 205 amino acids long with a molecular mass of 23 kDa. It has a predicted isoelectric point of 4.72. It is predicted to have a half-life around 30 hours. C20orf196 contains 19 positive residues (9.3%), 32 negative residues (15.6%), and 46 hydrophobic residues (22.4%).

Additionally, PDMS surfaces can be treated to render them either hydrophilic or hydrophobic, depending on the desired application. This versatility allows PDMS to be used in nearly all microfluidic applications. Despite its wide range of uses, there are instances where other materials are preferred. Glass is a common alternative when PDMS is not desirable.

Schematic illustration of a MSP nanodisc with a 7-transmembrane protein embedded. Diameter is about 10 nm. Picture from Sligar Lab A nanodisc is a synthetic model membrane system which assists in the study of membrane proteins. It is composed of a lipid bilayer of phospholipids with the hydrophobic edge screened by two amphipathic proteins.

The S2 sub-pocket is small, shallow and not well defined. It merges with the S4 subpocket. The S3 sub- pocket is located on the rim of the S1 pocket and is quite exposed to solvent. The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site.

Dephosphorylation of PKC at the hydrophobic motif by PHLPP allows PKC to be dephosphorylated at two other sites (the activation loop and the turn motif). This in turn renders PKC sensitive to degradation. Thus, prolonged increases in PHLPP expression or activity inhibit PKC phosphorylation and stability, decreasing the total levels of PKC over time.

If the benzyl group of silanediol is replaced by an i-butyl group it gives a weaker ACE inhibitor. Introduction of a hydrophobic methyl phenyl gives a little more potency than an analogue with a tert-butyl-group at P1. That suggests that methyl phenyl gives a better S1 recognition than a tert-butyl group.

Separation of cells is typically done using centrifugation, however foam separation has also been used as a more energy efficient technique. This method has been used on many species of bacteria cells such as Hansenula polymorph, Saccharomyces carlsbergensis, Bacillus polymyxa, Escherichia coli, and Bacillus subtilis, being most effective on cells that have hydrophobic surfaces.

Owing to its large surface area together with hydrophobic chains emerging from the clay surface, organoclay can be used to remove oil from water. It is also applied as a component in paint formulations or as a viscosifier for oil-based drilling fluids. It can be used in polymer chemistry as a nucleating agent.

Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found. This domain has disulphide isomerase activity. The function of the C-terminal is chaperone and dimerization.

The enzyme has a tendency to exist in the open conformation with short periods of closure and catalysis, which allow for rapid diffusion of substrate and products through the binding sites; the open conformation of PGK is more conformationally stable due to the exposure of a hydrophobic region of the protein upon domain closure.

The smallest bubbles entrained in the water column dissolve entirely, leading to higher ratios of dissolved gases in the surface ocean. The bubbles that do not dissolve eventually make it back to the surface. As they rise, these bubbles accumulate hydrophobic substances. Presence of dissolved organic matter stabilizes the bubbles, aggregating together as sea foam.

The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure. Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time.

Amidopropyl Hydroxysultaine, R= long hydrophobic tail Hydroxysultaines are chemical compounds used in high-foaming shampoos, bath products and shower gels especially in conjunction with ether sulfates and alkyl sulfates. They are also used in industrial applications where high, stable foam is required. Chemically, hydroxysultaines are zwitterionic, typically containing covalently linked positive and negative ions.

The structure of lactosylceramide. The Lactosylceramides, also known as LacCer, are a class of glycosphingolipids composed of a variable hydrophobic ceramide lipid and a hydrophilic sugar moiety. Lactosylceramides are found in microdomains on the plasma layers of numerous cells. Moreover, they are a type of ceramide including lactose, which is an example of a globoside.

Lymphocyte antigen 96 has been shown to interact with TLR 4. When LPS binds to a hydrophobic pocket in MD-2, it directly mediates dimerization of the two TLR4-MD-2 complexes. Thus, MD-2 form a heterodimer that recognizes a common pattern in structurally diverse LPS molecules. These interactions allow TLR4 to recognize LPS.

Nanocarriers discovered thus far include polymer conjugates, polymeric nanoparticles, lipid-based carriers, dendrimers, carbon nanotubes, and gold nanoparticles. Lipid-based carriers include both liposomes and micelles. Examples of gold nanoparticles are gold nanoshells and nanocages. Different types of nanomaterial being used in nanocarriers allows for hydrophobic and hydrophilic drugs to be delivered throughout the body.

It forms an olive green suspension. MoTe2 is hydrophobic, but the surfactant coats the surface with its lipophilic tail. The sheets in α-MoTe2 are able to be penetrated by alkali metals such as lithium to form intercalation compounds. This property means that it could be used as an electrode in a lithium battery.

The patterning of proteins has helped the advancement of biosensors., cell biology research, and tissue engineering. Various proteins have been proven to be suitable inks and are applied to various substrates using the microcontact printing technique. Polylysine, immunoglobulin antibody, and different enzymes have been successfully placed onto surfaces including glass, polystyrene, and hydrophobic silicon.

Mutually immiscible liquid phases are formed from water (aqueous phase), hydrophobic organic solvents, perfluorocarbons (fluorous phase), silicones, several different metals, and also from molten phosphorus. Not all organic solvents are completely miscible, e.g. a mixture of ethylene glycol and toluene may separate into two distinct organic phases. Phases do not need to macroscopically separate spontaneously.

Chemical structure of n-decyl-β-D-maltopyranoside (DM) Alkyl Maltosides are a class of detergents composed of a hydrophilic maltose and a hydrophobic alkyl chain. Variation in the alkyl chain confers a range of detergent properties including CMC and solubility. Maltosides are most often used for the solubilization and purification of membrane proteins.

When encapsulating hydrophobic or potentially toxic materials it is important that the encapsulant remain intact while inside the body. Studying the rheological properties of the micelles permits identification and selection of the polymer that is most appropriate for use in long-term biological applications. Rf-PEG exhibits superior rheological properties when used in vivo.

C12orf42 protein takes on several secondary structures, such as: alpha helices, beta sheets, and random coils. C12orf42 protein is a soluble. Proteins that are soluble have a hydrophilic outside and hydrophobic interior . Proteins with this type of structure are able to freely float inside a cell, due to the liquid composition of the cytosol.

As the temperature in the environment increases, molecules move faster. Hydrogen bonds and hydrophobic interactions are important stabilizing forces in proteins. If the temperature rises and molecules containing these interactions are moving too fast, the interactions become compromised or even break. At high temperatures, these interactions cannot form, and a functional protein is denatured.

Statine, an amino acid, is thought to be responsible for the inhibitory activity of pepstatin, because it mimics the tetrahedral transition state of the peptide catalysis. Because of hydrophobic properties of statine, pepstatin has very low solubility in physiological media. Since it had low potency and poor solubility, it did not enter in vivo studies.

T7 polymerase by itself has a very low processivity. It dissociates from the primer-template after incorporating about 15 nucleotides. Upon infection of the host, T7 polymerase binds to host thioredoxin in 1:1 ratio. The hydrophobic interaction between thioredoxin and T7 polymerase helps to stabilize the binding of T7 polymerase to primer-template.

Since these coatings are hydrophobic and repels water from the metal pipe and can also protect metal from salt water attack. Nanoparticle based systems can provide better adhesion and transparency. The TiO2 coating captures and breaks down organic and inorganic air pollutants by a photocatalytic process, which leads to putting roads to good environmental use.

The amino-terminal domains are not similar to reticulons within the family. However, the three-dimensional structure has been preserved from yeasts to plants to humans. The hydrophobic region of the structure is abnormally long compared to other transmembrane domains. The structure of the reticulon may be related to the function of this protein.

One finding suggests that the amino-acid terminus and the 66-loop extend into the extracellular space. This would indicate that the hydrophobic region double-backs on itself in the membrane. Other data suggests that the amino- terminal is intracellular. Lastly, a third model explains the 66-loop and amino-terminal domain are cytoplasmic.

Atractyloside is a hydrophilic glycoside. A modified glucose is linked to the hydrophobic diterpene atractyligenin by a β1-glycosidic bond. A carboxyl group is positioned at the C4 position in the axial position. The glucose part is esterified with isovaleric acid on the C2' atom, and sulfuric acid on the C3' and C4' atoms.

The F-G loop mediates the binding and passage of substrates, and its hydrophobic region containing residues Trp-235, Phe-239 and Ille-236 allows the enzyme to interact with cellular membranes. Mutations to hydrophilic residues in the F-G loop alter the binding mechanism by changing insertion depth of the enzyme into the membrane.

Surface eroding polymers do not allow water to penetrate into the material. They erode layer by layer, like a lollipop. The hydrophobic backbone with hydrolytically labile anhydride linkages allows hydrolytic degradation to be controlled by manipulating the polymer composition. This manipulation can occur by adding a hydrophilic group to the polyanhydride to make a copolymer.

ITP3K is regulated by various post-translational mechanisms. ITP3Ks are stimulated directly by calcium/calmodulin (Ca2+/CaM) binding. Generally, mammalian ITP3Ks are activated by calcium and calmodulin to varying degrees. The method in which this works is calmodulin recognizes sequences which contain amphiphilic alpha-helices with clusters of positively charged and hydrophobic amino acids.

Xenon is an effective inhibitor of plasma membrane Ca2+ ATPase. Xenon inhibits Ca2+ ATPase by binding to a hydrophobic pore within the enzyme and preventing the enzyme from assuming active conformations. Xenon is a competitive inhibitor of the serotonin 5-HT3 receptor. While neither anesthetic nor antinociceptive, this reduces anesthesia-emergent nausea and vomiting.

This is achieved by a ubiquitin interacting motif (UIM) found in a hydrophobic patch in the C-terminal region of the S5a/Rpn10 unit. Lysine 63-linked chains are not associated with proteasomal degradation of the substrate protein. Instead, they allow the coordination of other processes such as endocytic trafficking, inflammation, translation, and DNA repair.

These features are very important for new peptide design. Helical β-peptides mimic antimicrobial activities of host defense peptides. This feature requires the orientation of cationic –hydrophilic on one side, and hydrophobic residues on the other side of the helix. The attachment of fluorescent group on one head of the molecule confers contrast properties.

Internal sizing chemicals used in papermaking at the wet end are alkyl succinic anhydride (ASA), alkyl ketene dimer (AKD) and rosin. By making the paper web more hydrophobic, the sizing agents influence dewatering and retention of fillers and fibers in the paper sheet. Next to paper quality, internal sizing agents' main effect is on runability of the paper machine.

ClpS is an N-recognin in the N-end rule pathway. ClpS interacts with protein substrates that have a bulky hydrophobic residue (leucine, phenylalanine, tyrosine, and tryptophan) at the N-terminus. The protein substrate is then degraded by the ClpAP protease. In molecular biology, the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein.

Each subunit is a bundle of four right-handed α-helixes and has a molecular mass of 13.4 kDa (117 amino acids). The subunits align to give Ni-SOD a three-fold axis of symmetry. There are six nickel cofactors in total (one for each subunit). The subunits also have a hydrophobic core, which helps drive protein folding.

At the transition between this layer and the stratum corneum, cells secrete lamellar bodies (containing lipids and proteins) into the extracellular space. This results in the formation of the hydrophobic lipid envelope responsible for the skin's barrier properties. Concomitantly, cells lose their nuclei and organelles causing the granular cells to become non-viable corneocytes in the stratum corneum.

Cry6Aa has pore-forming action that destroys insect intestinal epithelial cells. Most Cry proteins have 3 domains, but Cry6Aa is composed largely of alpha helices, which indicates different membrane insertion methods. Cry6Aa has catalytic head domains regulated by hydrophobic residues. When Cry6Aa is first ingested, it remains a pro-toxin until intestinal proteases cleave the protein into active particles.

Nanocomposite hydrogels incorporated with polymeric nanoparticles are tailored for drug delivery and tissue engineering. The addition of polymeric nanoparticles gives these hydrogels a reinforced polymeric network that is more stiff and has the ability to enclose hydrophilic and hydrophobic drugs along with genes and proteins. The high stress-absorbing property makes them a potential candidate for cartilage tissue engineering.

Biomass, (1990). 23(4): p. 289-305. Recovery can be achieved by filtration or centrifugation. Due to the hydrophobic nature of organosolv lignin, flotation of organosolv lignin is effective without the use of the collecting and precipitating agentsMacfarlane, AL, Prestidge, R, Farid, MM, Chen, JJJ, Dissolved air flotation: A novel approach to recovery of organosolv lignin.

Surfactants are composed of a polar head group that is hydrophilic and a nonpolar tail group that is hydrophobic. The head groups can be anionic, cationic, zwitterionic, or nonionic. The tail group can be a hydrocarbon, fluorocarbon, or a siloxane. Extensive variation in the surfactant’s solution and interfacial properties is allowed through different molecular structures of surfactants.

It is encoded by all codons starting with GU (GUU, GUC, GUA, and GUG). Like leucine and isoleucine, valine is a branched-chain amino acid. In sickle-cell disease, a single glutamic acid in β-globin is replaced with valine. Because valine is hydrophobic, whereas glutamic acid is hydrophilic, this change makes the hemoglobin prone to abnormal aggregation.

General structure of the CREB protein. CREB proteins are activated by phosphorylation from various kinases, including PKA, and Ca2+/calmodulin-dependent protein kinases on the Serine 133 residue. When activated, CREB protein recruits other transcriptional coactivators to bind to CRE promoter 5’ upstream region. Hydrophobic leucine amino acids are located along the inner edge of the alpha helix.

The Kitchen as Laboratory: Reflections on the Science of Food and Cooking. New York: Columbia University Press. 142–145 This instability is caused by interactions between hydrophobic molecules and charged molecules within the ketchup suspension. Pectin is a polysaccharide within tomatoes that has the ability to bind to itself and to other molecules, especially water, around it.

High heat (such as the sustained high temperatures above 72 °C associated with the pasteurization process) denatures whey proteins. While native whey protein does not aggregate upon renneting or acidification of milk, denaturing the whey protein triggers hydrophobic interactions with other proteins, and the formation of a protein gel. Heat-denatured whey can still cause allergies in some people.

Endocannabinoids are hydrophobic molecules. They cannot travel unaided for long distances in the aqueous medium surrounding the cells from which they are released and therefore act locally on nearby target cells. Hence, although emanating diffusely from their source cells, they have much more restricted spheres of influence than do hormones, which can affect cells throughout the body.

Peramivir has a guanidino group similar to zanamivir and a hydrophobic group similar to oseltamivir. Mutations that effect the efficiency of oseltamivir and zanamivir can also effect peramivir efficiency. Resistances to peramivir have been seen at the mutation of H274Y residue in vitro. One of these resistances is associated with cross-resistance to peramivir and oseltamivir.

Examples of amphiphilic compounds are the salts of fatty acids, phospholipids. Many simple amphiphiles are used as detergents. A mixture of soap and water is an everyday example of a lyotropic liquid crystal. Biological structures such as fibrous proteins showings relatively long and well-defined hydrophobic and hydrophilic ‘‘blocks’’ of aminoacids can also show lyotropic liquid crystalline behaviour.

The structure has been shown to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core similar to that of C-type lectin. This domain contains four conserved cysteines involved in two disulphide bonds. The link domain has also been termed HABM (hyaluronic acid binding module) and PTR (proteoglycan tandem repeat).

HCV genome E1 is one of two subunits of the envelope glycoprotein found in the hepatitis C virus. The other subunit is E2. This protein is a type 1 transmembrane protein with a highly glycosylated N-terminal ectodomain and a C-terminal hydrophobic anchor. After being synthesized the E1 glycoproteins associates with the E2 glycoprotein as a noncovalent heterodimer.

OSBP is the founding member of the ORP (OSBP-related proteins) family of lipid transfer proteins. Mammals have 16 different ORPs, whereas the yeast S. cerevisiae genome encodes seven ORP homologues (Osh). ORP and Osh proteins contain a lipid transport domain called ORD (OSBP-related domain) encompassing the EQVSHHPP signature sequence. The ORD structure consists in a hydrophobic pocket.

Structure of sensory rhodopsin II is typical for microbial rhodopsin. It consists of seven transmembrane a-helices with retinal molecule connected via Schiff base to K205. Notable feature of sensory rhodopsin II is presence of charged residue Y199 on the surface of the hydrophobic region. This residue is responsible for binding of sensory rhodopsin II transducer protein - HtrII.

Serralysin (, Pseudomonas aeruginosa alkaline proteinase, Escherichia freundii proteinase, Serratia marcescens extracellular proteinase, Serratia marcescens metalloproteinase, Pseudomonas aeruginosa alk. protease, Serratia marcescens metalloprotease) is an enzyme. This enzyme catalyses the following chemical reaction : Preferential cleavage of bonds with hydrophobic residues in P1' This extracellular endopeptidase is present in Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi.

While the phenyl and ethyloxyphenyl groups form hydrophobic interactions. The aryloxy propylamine moiety is also found in many other monoamine reuptake inhibitors, but the placement of substituents on the phenyl ring determine the selectivity. Compounds with substituents in position 2’ have selectivity for NET. Compounds with substituents in position 4’ are selective serotonin reuptake inhibitors e.g.

The blood brain barrier restricts diffusion to small hydrophobic molecules, making drug diffusion difficult to achieve. Blood flow is directly influenced by the thermodynamics of the body. Changes in temperature affect the viscosity and surface tension of the blood, altering the minimum blood flow rate. At high temperatures the minimum flow rate will decrease and the capillary will expand.

This makes it very difficult to get drugs into the brain without invasively administering them directly into the brain. One possible solution is the utilization of nanoparticles. Nanoparticles are synthesized to encapsulate a target drug. The surface of the nanoparticle, if not already hydrophobic, may have polymers attached to the surface to adjust the current polarity.

The first and second helices interact with the serine/threonine kinase Raf-1 and the second and third helices are the sites of the BAG domain interaction with the ATPase domain of Hsc70/Hsp70. Binding of the BAG domain to the ATPase domain is mediated by both electrostatic and hydrophobic interactions in BAG-1 and is energy requiring.

1-Butyl-3-methylimidazolium hexafluorophosphate, also known as BMIM-PF6, is a viscous, colourless, hydrophobic and non-water-soluble ionic liquid with a melting point of -8 °C. Together with 1-butyl-3-methylimidazolium tetrafluoroborate, BMIM-BF4, it is one of the most widely studied ionic liquids. It is known to very slowly decompose in the presence of water.

In 1998, a new form of MMC, hydrophobic charge induction chromatography (HCIC), was proposed by Burton and Harding. S.C. Burton, D.R.K. Harding, J. Chromatogr. A 814 (1998) 71. In the same year, conjoint liquid chromatography (CLC), which combines different types of monolithic convective interaction media (CIM) disks in the same housing, was introduced by Štrancar et al.

The Sec14 protein was the first CRAL-TRIO domain for which the structure was determined. The structure contains several alpha helices as well as a beta sheet composed of 6 strands. Strands 2,3,4 and 5 form a parallel beta sheet with strands 1 and 6 being anti-parallel. The structure also identified a hydrophobic binding pocket for lipid binding.

Plasmepsin II (, aspartic hemoglobinase II, PFAPD) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr This enzyme is present in malaria organism, Plasmodium.

Phytepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-Asp- and -Asp-Asp- bonds in 2S albumin from plant seeds This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert.

The effects of TMAO on the backbone and charged residues of peptides are found to stabilize compact conformations, whereas effects of TMAO on nonpolar residues lead to peptide swelling. This suggests competing mechanisms of TMAO on proteins, which accounts for hydrophobic swelling, backbone collapse, and stabilization of charge-charge interactions. These mechanisms are observed in Trp cage.

The molecular weight of FAM76A is 38.4 kDa, making it possible for this protein to diffuse through nuclear pores. The isoelectric point is 9.28. FAM76A does not have any significant positive, negative, or mixed charge clusters. In addition, FAM76A does not have any predicted hydrophobic or transmembrane segments, suggesting that this protein is not found within the cell membrane.

Guanidinium chloride is a strong chaotrope and one of the strongest denaturants used in physiochemical studies of protein folding. It also has the ability to decrease enzyme activity and increase the solubility of hydrophobic molecules. At high concentrations of guanidinium chloride (e.g., 6 M), proteins lose their ordered structure, and they tend to become randomly coiled, i.e.

The interactions between the protein and ligand substantially affect the specificity between the two entities. Electrostatic interactions and Hydrophobic interactions are known to be the most influential in regards to where specificity between two molecules is derived from. The strength of these interactions between the protein and ligand positively correlate with their specificity for one another.

The mechanism of this process is not fully understood, but involves the recognition and processing by the translocon of hydrophobic stretches in the amino acid sequence which are destined to become transmembrane helices. Closed by stop- transfer sequences and opened by embedded signal sequences, the plug alters between its open and closed states to place helices in different orientations.

The type of interactions that occurs to reassemble peptide structures include van der Waals forces, ionic bonds, hydrogen bonds and hydrophobic forces. These forces also facilitate the molecular recognition function that the peptides encompasses. These interactions works on a basis of preference dependent on energy properties and specificity. A range of different nanostructures can be formed.

Cl-PAHs are hydrophobic compounds and their persistence within ecosystems is due to their low water solubility. They are structurally similar to other halogenated hydrocarbons such as polychlorinated dibenzo-p-dioxins (PCDDs), dibenzofurans (PCDFs), and polychlorinated biphenyls (PCBs). Cl-PAHs in the environment are strongly susceptible to the effects of gas/particle partitioning, seasonal sources, and climatic conditions.

The hydrophobic N-terminus of Sar1-GTP then locates it to the membrane, where it serves as the binding site for the Sec23/Sec24 protein coat complex. After the vesicle coat is completely assembled and the vesicle is released from the donor membrane, the Sec23 subunit promotes Sar1 GTPase activity, which triggers the disassembly of the COPII coat.

1-Hexadecanethiol is used as a synthesis chemical. The compound is also used for the production of nanoparticles and hydrophobic self-assembling monolayers. The high affinity of the thiol group to the elements of the copper group causes the thiols to spontaneously deposit in a high-order layer when a corresponding metal of a 1-hexadecanethiol solution is exposed.

The water-soluble MβCD is known to form soluble inclusion complexes with cholesterol, thereby enhancing its solubility in aqueous solution. MβCD is employed for the preparation of cholesterol-free products: the bulky and hydrophobic cholesterol molecule is easily lodged inside cyclodextrin rings. MβCD is also employed in research to disrupt lipid rafts by removing cholesterol from membranes.

One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues. Leucine-rich repeats are frequently involved in the formation of protein–protein interactions.

The organic substituents also define a hydrophobic pocket around the reactive coordination site. Stoichiometric and catalytic applications of pincer complexes have been studied at an accelerating pace since the mid-1970s. Most pincer ligands contain phosphines.Jensen, C. M., "Iridium PCP pincer complexes: highly active and robust catalysts for novel homogeneous aliphatic dehydrogenations", Chemical Communications, 1999, 2443–2449. .

Video of water striders The family Gerridae is physically characterized by having hydrofuge hairpiles, retractable preapical claws, and elongated legs and body. Hydrofuge hairpiles are small, hydrophobic microhairs. These are tiny hairs with more than one thousand microhairs per mm. The entire body is covered by these hairpiles, providing the water strider resistance to splashes or drops of water.

This reduces the effects of photo-oxidation of surfaces. Hydrophobic and lipophobic ligands grafted to nanoparticles in coating One of the newer additions to this ever growing market are nanoparticle based coatings. Silica particles are formed using the sol-gel method. The resulting silica particles have both reactive (Si-OH) and nonreactive (Si=O) groups on the surface.

Its main use in pharmaceutics is with enteric formulations. It can be used together with other coating agents, e.g. ethyl cellulose. Cellulose acetate phthalate is commonly plasticized with diethyl phthalate, a hydrophobic compound, or triethyl citrate, a hydrophilic compound; other compatible plasticizers are various phthalates, triacetin, dibutyl tartrate, glycerol, propylene glycol, tripropionin, triacetin citrate, acetylated monoglycerides, etc.

Covalent interactions are those with the strongest association and are formed by disulphide bonds or electron sharing. While rare, these interactions are determinant in some posttranslational modifications, as ubiquitination and SUMOylation. Non-covalent bonds are usually established during transient interactions by the combination of weaker bonds, such as hydrogen bonds, ionic interactions, Van der Waals forces, or hydrophobic bonds.

Glycoproteins form broad, fuzzy bands in SDS-PAGE (Laemmli- electrophoresis) because of their broad distribution of negative charges. Using positively charged detergents such as CTAB will avoid issues associated with glycoproteins. Proteins can be blotted from CTAB-gels in analogy to western blots ("eastern blot"), and Myelin-associated high hydrophobic protein can be analyzed using CTAB 2-DE.

The gold region of the nanocoral surface was used for detecting and imaging. Thus, the targeting and sensing mechanisms were decoupled and could be separately engineered for a particular experiment. Additionally, the polystyrene region may also be used as a carrier for drugs and other chemicals by surface hydrophobic adsorption or encapsulation, making the nanocoral a possible multifunctional nanosensor.

Icosane's size, state or chemical inactivity does not exclude it from the traits its smaller alkane counterparts have. It is a colorless, non-polar molecule, nearly unreactive except when it burns. It is less dense than and insoluble in water. Its non- polar trait means it can only perform weak intermolecular bonding (hydrophobic/van der Waals forces).

These are microbial-synthesized surface-active substances that allow for more efficient microbial biodegradation of hydrocarbons in bioremediation processes. There are two ways by which biosurfactants are involved in bioremediation. (1) Increase the surface area of hydrophobic water-insoluble substrates. Growth of microbes on hydrocarbons can be limited by available surface area of the water-oil interface.

G. candidum reduces the bitterness in Camembert cheese through the activity of the aminopeptidases that hydrolyze low molecular weight hydrophobic peptides. Aminopeptidases also contributes an aroma in traditional Norman Camembert. The fungus also neutralizes the curd by catabolizing lactic acid produced by bacteria. G. candidum prepares the cheese for colonization of other acid sensitive bacteria such as Brevibacterium.

A common household product, Rain-X, utilizes SAMs to create a hydrophobic monolayer on car windshields to keep them clear of rain. Another application is an anti-adhesion coating on nanoimprint lithography (NIL) tools and stamps. One can also coat injection molding tools for polymer replication with a Perfluordecyltrichlorosilane SAM. Thin film SAMs can also be placed on nanostructures.

The first 250 residues of EF and LF have an irregular alternating sequence of basic, acidic, and hydrophobic residues. The interplay between the phenylalanine clamp and the protonation state cause a ratcheting effect that drives the protein though until enough has crossed into the cytoplasm to drag the rest through the pore as the N-terminus refolds (Fig. 11).

Molecular tweezers are host molecules capable of holding items between their two arms. The open cavity of the molecular tweezers binds items using non-covalent bonding including hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, π interactions, or electrostatic effects. Examples of molecular tweezers have been reported that are constructed from DNA and are considered DNA machines.

Microsomal prostaglandin E synthase type-2 (mPTGES2) has been crystallized with an anti- inflammatory drug indomethacin (IMN). The N-terminal of mPTGES2 is attached to the lipid membrane and the two hydrophobic pockets connected to form a V shape are located in the bottom of a large cavity for IMN binding. The mPTGES2 exists in a dimer.

Dolfin released its Titanium Tech suit in January 2015. The high-tech suit's "4-stage framing system" employs welding to control major muscle groups and to stabilize water displacement zones, compression liner that targets large muscle zones, woven fibers to increase strength and decrease weight, and hydrophobic-coated fibers to repel water - reducing water absorbency and drag.

Membrane distillation (MD) is a thermally driven separation process in which separation is driven by phase change. A hydrophobic membrane presents a barrier for the liquid phase, allowing the vapour phase (e.g. water vapour) to pass through the membrane's pores. The driving force of the process is a partial vapour pressure difference commonly triggered by a temperature difference.

Teflon is hydrophobic and chemically inert, making it a highly suitable material, and the most commonly used for troughs today. Occasionally metal or glass troughs coated with a thin layer of Teflon are used; however they are not as enduring as solid PTFE troughs.Chechel, O. V., & Nikolaev, E. N. (1991). Devices for production of Langmuir–Blodgett films - review.

Tetraphenylporphyrin, abbreviated TPP or H2TPP, is a synthetic heterocyclic compound that resembles naturally occurring porphyrins. Porphyrins are dyes and cofactors found in hemoglobin and cytochromes and are related to chlorophyll and vitamin B12. The study of naturally occurring porphyrins is complicated by their low symmetry and the presence of polar substituents. Tetraphenylporphyrin is hydrophobic, symmetrically substituted, and easily synthesized.

Specifically, the positively charged arginine and the non-polar alanine residues were both shown to be essential for poneratoxin potency. See figure, where the hydrophobic (red) and hydrophillic (blue) regions of poneratoxin and the lipid bilayer align, demonstrating that the structure is evolved to insert into the membrane, which will promote interaction with the voltage gated sodium channels.

In solution the dimeric form is present; the ratio of dimerisation is strongly dependent on the polarity of the solvent. Polar and protic solvents interact with the hydrogen bonds and more monomer is formed. Hydrophobic effects in non-polar solvents lead to a predominance of the dimer. The ratio of the tautomeric forms is also dependent on the solvent.

Nymphs of many fulgoroids produce wax from special glands on the abdominal terga and other parts of the body. These are hydrophobic and help conceal the insects. Adult females of many families also produce wax which may be used to protect eggs.C. H. Dietrich in Resh, V. H. & Carde, R. T. (Eds.) 2003 Encyclopedia of Insects.

Asphalt was used starting in the 1960s as a hydrophobic matrix aiming to encapsulate radioactive waste such as medium-activity salts (mainly soluble sodium nitrate and sodium sulfate) produced by the reprocessing of spent nuclear fuels or radioactive sludges from sedimentation ponds.Rodier, J., Scheidhauer, J., & Malabre, M. (1961). The conditioning of radioactive waste by bitumen (No. CEA-R1992).

Aminopeptidase S (, Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues This enzyme contains two zinc molecules in its active site and is activated by Ca2+.

Subunits must be of the same subfamily to form the multimeric protein channel. The tertiary structure of the channel allows ions to flow through the hydrophobic plasma membrane. Connexons are an example of a homomultimeric protein composed of six identical connexins. A cluster of connexons forms the gap-junction in two neurons that transmit signals through an electrical synapse.

Phospholipid arrangement in cell membranes. Phosphatidylcholine is the major component of lecithin. It is also a source for choline in the synthesis of acetylcholine in cholinergic neurons. Phospholipids (PL) are a class of lipids whose molecule has a hydrophilic "head" containing a phosphate group, and two hydrophobic "tails" derived from fatty acids, joined by an alcohol residue.

The glass cleans itself in two stages. The "photocatalytic" stage of the process breaks down the organic dirt on the glass using ultraviolet light and makes the glass superhydrophilic (normally glass is hydrophobic). During the following "superhydrophilic" stage, rain washes away the dirt, leaving almost no streaks, because water spreads evenly on superhydrophilic surfaces.BBC News, 8 June 2004.

There are many types of passive samplers used that specialize in absorbing different classes of aquatic contaminants found in the environment. Chemcatcher and SMPD are two types of passive samplers that are also commonly used. Monitoring programs use SMPDs to measure to hydrophobic organic contaminants. SPMDs are designed to mimic the bioconcentration of contaminants in fatty tissues (ITRC, 2006).

The Bacillus firmus transporter and several homologues examined have strongly charged, hydrophilic N-terminal domains (cytoplasmic) followed by a hydrophobic C-terminal domain with 5 putative transmembrane α-helical spanners. A central 100 residues resembles archaeal inositol monophosphate dehydrogenases. Kehres and Maguire suggest that the MgtE proteins are secondary carriers with inwardly directed polarity. Hattori et al.

This first report of electronic integration for paper-based microfluidics illustrated how this material can improve the design of these µTAS due its flexibility and low- cost. Coupling electronic components into the hydrophobic channels created on the paper-based microfluidic devices are based upon physical and chemical integration techniques; these two strategies are discussed in the sections below.

A MMP7 protein is bounded by four metal ions including a catalytic zinc ion, a structural zinc ion, and two calcium ions. The catalytic zinc ion binds to three His residues in the HEXGHXXGXXH region in tetracoordination. The calcium ion binding play important role in stabilizing the secondary structure. MMP7 has a shallow hydrophobic substrate-binding pocket.

The site of endothelial lipase enzymatic activity is the surface of endothelial cells. LIPG regulates lipoprotein metabolism through the hydrolysis of HDL phospholipds. This high-density lipoprotein is an amphipathic lipid, meaning the lipid is composed of both a hydrophobic and a hydrophilic component. Cholesterol has a four-ring structure and is an isoprenoid-based hydrocarbon.

The structure of mtFabH. The enzyme is a homodimer of mixed α-helices and β-sheets, or a thiolase fold. The catalytic triads of C122, H258, and N289 are shown in colour and are largely buried in hydrophobic pockets. Crystal structures of FabH have been reported from Mycobacterium tuberculosis,{, , ; ; Staphylococcus aureus,; Escherichia coli,; and Thermus thermophilus.

ATAT1 contains a conserved surface pocket close to the active site composed largely of hydrophobic and basic residues, which likely complement the acidic loop containing α-tubulin K40. The protein's active site contains several conserved residues that could potentially function as general bases in the reaction: glutamine 58 (Q58), cysteine (C120), and aspartic acid 157 (D157).

Assembly of organs, tissues, cells and subcellular components are in part determined by their physical properties. For example, the cell membrane that forms a barrier between the inside and outside of the cell is a lipid bilayer that forms as result of the thermodynamic properties of the phospholipids it's made of (hydrophilic head and hydrophobic tails).

For example, if the blades are hydrophobic, water molecules do not bind to them, and the propellers can pump them well. If the blades are hydrophilic, water molecules form hydrogen bonds with the atoms in the polar blades. This can largely block the flow of other water molecules around the blades and significantly slow down their pumping.

Many sulfate esters are used in detergents, and some are useful reagents. Alkyl sulfates consist of a hydrophobic hydrocarbon chain, a polar sulfate group (containing an anion) and either a cation or amine to neutralize the sulfate group. Examples include: sodium lauryl sulfate (also known as sulfuric acid mono dodecyl ester sodium salt) and related potassium and ammonium salts.

A large conformational change reveals a large hydrophobic interface that allows for subunit rotation which may be driven by superhelical torsion within the protein-DNA complex. After this 180° rotation, Hin returns to its native conformation and re-ligates the cleaved DNA, without the aid of high energy cofactors and without the loss of any DNA.

In PDE1 this region contains a calmodulin binding domain. The catalytic domains of PDE1 (and other types of PDEs) have three helical subdomains: an N-terminal cyclin-fold region, a linker region and a C-terminal helical bundle. A deep hydrophobic pocket is formed at the interface of these subdomains. It is composed of four subsites.

Another strategy to minimise membrane fouling is the use of the appropriate membrane for a specific operation. The nature of the feed water must first be known; then a membrane that is less prone to fouling with that solution is chosen. For aqueous filtration, a hydrophilic membrane is preferred. For membrane distillation, a hydrophobic membrane is preferred.

The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein.

Wnt ligands are classically described as acting in an autocrine/paracrine manner. Wnts are also hydrophobic with significant post-translational palmitoylation and glycosylation. These post-translational modifications are important for docking to extracellular lipoprotein particles allowing them to travel systemically. Additionally, due to the high degree of sequence homology between Wnts many are characterized by their downstream actions.

Illustration of lipid vesicles fusing showing two possible outcomes: hemifusion and full fusion. In hemifusion only the outer bilayer leaflets mix. In full fusion both leaflets as well as the internal contents mix. In membrane biology, fusion is the process by which two initially distinct lipid bilayers merge their hydrophobic cores, resulting in one interconnected structure.

Lipocalin-1 is a protein that in humans is encoded by the LCN1 gene. The protein encoded by this gene belongs to the lipocalin family. Lipocalins are a group of extracellular proteins that are able to bind lipophiles by enclosure within their structures to minimize solvent contact. This protein may bind hydrophobic ligands and inhibit cysteine proteinases.

SK potassium channels share the same basic architecture with Shaker-like voltage-gated potassium channels. Four subunits associate to form a tetramer. Each of the subunits has six transmembrane hydrophobic alpha helical domains (S1-S6). A loop between S5 and S6—called the P-loop—provides the pore-forming region that always faces the center of the channel.

The heavy chain has a hydrophobic section near the N-terminus that supports the transmembrane anchor. The heavy chain influences the specificity of enteropeptidase. Native enteropeptidase is resistant to soybean trypsin inhibitor. However, the isolated light chain is subtle whether prepared by limited reduction of the natural protein or by mutagenesis and expression in COS cells.

A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water.

The hydrophobic structure prevents the electrolyte from leaking into the reactant gas flow channels and ensures diffusion of the gases to the reaction site. The two layers are then pressed onto a conducting metal mesh, and sintering completes the process. Further variations on the alkaline fuel cell include the metal hydride fuel cell and the direct borohydride fuel cell.

Trypanosoma brucei gambiense causes 97% of human cases of sleeping sickness. Resistance to ApoL1 is principally mediated by the hydrophobic ß-sheet of the T. b. gambiense specific glycoprotein. Other factors involved in resistance appear to be a change in the cysteine protease activity and TbHpHbR inactivation due to a leucine to serine substitution (L210S) at codon 210.

Reactants and products likely enter and leave the active site through a hydrophobic tunnel which is thought to open into the lipid membrane for direct lipid substrate absorption. A second, smaller tunnel also reaches the active site and may serve as a pathway for water, but is too narrow to transport the retinoid reactants and products.

They are usually organized into a bilayer in membranes with the polar hydrophillic heads sticking outwards to the aqueous environment and the non polar hydrophobic tails pointing inwards. Glycerophospholipids consists of various diverse species which usually differ slightly in structure. The most basic structure is a phosphatidate. This species is an important intermediate in the synthesis of many phosphoglycerides.

Shikimate dehydrogenase also has an NADPH binding site that contains a Rossmann fold. This binding site normally contains a glycine P-loop. The domains of the monomer show a fair amount of flexibility suggesting that the enzyme can open in close to bind with the substrate 3-Dehydroshikimate. Hydrophobic interactions occur between the domains and the NADPH binding site.

The cleavage is catalysed by a protease within the C-terminal domain. During the reaction a cholesterol molecule is added to the C-terminus of SHH-N. Thus the C-terminal domain acts as an intein and a cholesterol transferase. Another hydrophobic moiety a palmitate is added to the alpha- amine of N-terminal cysteine of SHH-N.

This interaction is significantly stabilized by many ionic and hydrogen bonds that take place between the residues of three interacting polypeptide chains adjacent to the central hydrophobic patch. This specificity is most likely due to the lack of conformational flexibility of the binding fragment of E3BP and the complementary amino acid match with the E3 interface.

BEV has a crater-like depression at the icosahedral 5-fold axis which descends into a cylindrical hole of 10 Å in diameter which runs almost to the inner surface of the capsid. A hydrophobic pocket contained within VP1 contains a myristic acid molecule, the removal of which appears to be a prerequisite for virus uncoating.

Proposed mechanism of peptide cleavage by aspartyl proteases. Aspartyl proteases are a highly specific family of proteases – they tend to cleave dipeptide bonds that have hydrophobic residues as well as a beta-methylene group. Unlike serine or cysteine proteases these proteases do not form a covalent intermediate during cleavage. Proteolysis therefore occurs in a single step.

A putative catalytic residue in the A1 fragment (Glu112) lies close to a hydrophobic region, which packs two loops together. It is thought that this region might be important for catalysis and membrane translocation. The structural arrangement of E. coli type I and type II heat-labile enterotoxins are very similar, although they are antigenically distinct.

PLFA analysis may be combined with other techniques, such as stable isotope probing to determine which microbes are metabolically active in a sample. PLFA analysis was pioneered by D.C. White at the University of Tennessee, in the early to mid 1980s. Phospholipid bilayer. Each phospholipid consists of a polar hydrophilic head (red) and two hydrophobic fatty acid tails.

23% in deciduous trees. Lignin confers the hydrophobic properties reflecting the fact that it is based on aromatic rings. These three components are interwoven, and direct covalent linkages exist between the lignin and the hemicellulose. A major focus of the paper industry is the separation of the lignin from the cellulose, from which paper is made.

Mating factor receptors STE2 and STE3 are integral membrane proteins that may be involved in the response to mating factors on the cell membrane. The amino acid sequences of both receptors contain high proportions of hydrophobic residues grouped into 7 domains, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins.

Another unusual phenomenon is a 7-figure periodic element of a negatively charged amino acid followed by six other hydrophobic amino acids, which occurs six times within the protein when compared to the swp23s.q dataset. There are two instances of Serine spacing and two instances of Phenylalanine spacing that comprise unusually large distances when compared to the swp23s.q dataset.

The main structural elements involved in the mollusk shell formation process are: a hydrophobic silk gel, aspartic acid rich protein, and a chitin support. The silk gel is part of the protein portion and is mainly composed of glycine and alanine. It is not an ordered structure. The acidic proteins play a role in the configuration of the sheets.

The α1 subunit has four homologous domains, each with six transmembrane segments. Within each homologous domain, the fourth transmembrane segment (S4) is positively charged, as opposed to the other five hydrophobic segments. This characteristic enables S4 to function as the voltage-sensor. Alpha-1D subunits belong to the Cav1 family, which is characterised by L-type calcium currents.

The fusogens of classes I–III have many structural differences. However, the method they utilize to induce membrane fusion is mechanistically similar. When activated, all of these fusogens form elongated trimeric structures and bury their fusion peptides into the membrane of the target cell. They are secured in the viral membrane by hydrophobic trans-membrane regions.

Otherwise, van-der- Waals forces, pi-pi-interactions or hydrophobic interactions might stabilize the extractant inside the particle pores. However, the possible decrease of extractant loss depends largely on the pore size and the water solubility of the extractant. Nonetheless, SIRs have a significant advantage over e.g. custom made ion-exchange resins with chemically bonded ligands.

This phenolic bislactones has been shown to have potent tumor promoting activities. Debromoaplysiatoxin produces erythema, blisters and necrosis. The dehydrated anhydrotoxins of debromoaplysiatoxin are relatively nontoxic. Examination of the structure–activity relationship (SAR) of this hydrophobic region showed that the absence of the brominated molecule in moieties of Lyngbya toxins reduced malignant transformation and DNA synthesis in cells.

Cobalt oxide is often obtained by hydrothermal synthesis in an autoclave. One-pot hydrothermal synthesis of metal oxide hollow spheres starts with carbohydrates and metal salts dissolved in water at 100-200 °C. The reaction produces carbon spheres, with metal ions integrated into the hydrophobic shell. The carbon cores are removed by calcination, leaving hollow metal oxide spheres.

Devices used to sample the concentrations of particulates and compounds of the SML include a glass fabric, metal mesh screens, and other hydrophobic surfaces. These are placed on a rotating cylinder which collects surface samples as it rotates on top of the ocean surface.Harvey, George W. (1966). Microlayer Collection from the Sea Surface: A New Method and Initial Results.

Cord factor's amphiphilic nature leads to varying structures when many cord factor molecules are in close proximity. On a hydrophobic surface, they spontaneously form a crystalline monolayer. This crystalline monolayer is extremely durable and firm; it is stronger than any other amphiphile found in biology. This monolayer also forms in oil-water, plastic-water, and air-water surfaces.

Peptide amphiphiles (PAs) are peptide-based molecules that self-assemble into supramolecular nanostructures including; spherical micelles, twisted ribbons, and high-aspect-ratio nanofibers. A peptide amphiphile typically comprises a hydrophilic peptide sequence attached to a lipid tail, i.e. a hydrophobic alkyl chain with 10 to 16 carbons. Therefore, they can be considered a type of lipopeptide.

Researchers have found that although metallic iron nanoparticles remediate contaminants well, they tend to agglomerate on the soil surfaces. In response, carbon nanoparticles and water- soluble polyelectrolytes have been used as supports to the metallic iron nanoparticles. The hydrophobic contaminants adsorb to these supports, improving permeability in sand and soil. In field tests have generally confirmed lab findings.

They showed that human beta interferon was an unusually hydrophobic glycoprotein. This explained the large loss of interferon activity when preparations were transferred from test tube to test tube or from vessel to vessel during purification. The analyses showed the reality of interferon activity by chemical verification. The purification of human alpha interferon was not reported until 1978.

The last exon of TNMD gene encodes the conserved C-terminal cysteine-rich domain, which makes up the part of the protein sharing highest resemblance to chondromodulin-I (77% similarity/66% identity). This domain contains C-terminal hydrophobic tail with eight Cys residues forming four disulphide-bridges, which are well conserved across vertebrate species. A smaller cyclic structure forming by single Cys280-Cys292 disulphide bridge in TNMD has been shown to exert an anti-angiogenic function, while the other three disulphide-bridges are speculated to hold this cyclic structure and C-terminal hydrophobic tail separated from each other to avoid the formation of intramolecular aggregates. In certain tendon tissues such as Achilles tendon and chordae tendineae cordis, 16 kDa cleaved C-terminal part of TNMD was detected in the collagenous extracellular matrix.

Dynorphins (Dyn) are a class of opioid peptides that arise from the precursor protein prodynorphin. When prodynorphin is cleaved during processing by proprotein convertase 2 (PC2), multiple active peptides are released: dynorphin A, dynorphin B, and α/β-neo-endorphin. Depolarization of a neuron containing prodynorphin stimulates PC2 processing, which occurs within synaptic vesicles in the presynaptic terminal. Occasionally, prodynorphin is not fully processed, leading to the release of “big dynorphin.” “Big Dynorphin” is a 32-amino acid molecule consisting of both dynorphin A and dynorphin B. Dynorphin A, dynorphin B, and big dynorphin all contain a high proportion of basic amino acid residues, in particular lysine and arginine (29.4%, 23.1%, and 31.2% basic residues, respectively), as well as many hydrophobic residues (41.2%, 30.8%, and 34.4% hydrophobic residues, respectively).

Cupiennin 1 family is the more well-known group, and consists of at least four peptides, such as cupiennin 1a, 1b, 1c, and 1d. Cupiennin 1a (M-ctenitoxin-Cs1a) is the most abundant and has a molecular mass of 3798.63 Da. Cupiennin 1b is less abundant and has a size of 3800.25 Da. Cupiennin 1c (3769.75 Da) and 1d (3795.13) are in extremely low concentrations. These peptides are highly cationic, made up of similar amino acids, but different in the N- and C-terminal ends. The hydrophobic N-terminal is characterised by six repeats of four amino acids, which are in a conserved sequence: position 1 is always lysine; position 2 is variable; position 3 is always a hydrophobic amino acid or glycine, and in position 4 is either alanine or valine.

Within the cell, the process of GroEL/ES mediated protein folding involves multiple rounds of binding, encapsulation, and release of substrate protein. Unfolded substrate proteins bind to a hydrophobic binding patch on the interior rim of the open cavity of GroEL, forming a binary complex with the chaperonin. Binding of substrate protein in this manner, in addition to binding of ATP, induces a conformational change that allows association of the binary complex with a separate lid structure, GroES. Binding of GroES to the open cavity of the chaperonin induces the individual subunits of the chaperonin to rotate such that the hydrophobic substrate binding site is removed from the interior of the cavity, causing the substrate protein to be ejected from the rim into the now largely hydrophilic chamber.

Despite the chemical diversity of NNRTIs they all bind at the same site in the RT. The binding occurs allosterically in a hydrophobic pocket located approximately 10 Å from the catalytic site in the palm domain of the p66 subunit site of the enzyme. The NNRTI binding pocket (NNIBP) contains five aromatic (Tyr-181, Tyr-188, Phe-227 and Trp-229), six hydrophobic (Pro-59, Leu-100, Val-106, Val-179, Leu-234 and Pro-236) and five hydrophilic (Lys-101, Lys-103, Ser-105, Asp-132 and Glu-224) amino acids that belong to the p66 subunit and additional two amino acids (Ile-135 and Glu-138) belonging to the p51 subunit. Each NNRTI interacts with different amino acid residues in the NNIBP. Figure 2 Chemical structure of nevirapine and the two wings.

The simplicity of the hydrophobic-polar model has caused it to have several problems that people have attempted to correct with alternative lattice protein models. Chief among these problems is the issue of degeneracy, which is when there is more than one minimum energy conformation for the modeled protein, leading to uncertainty about which conformation is the native one. Attempts to address this include the HPNX model which classifies amino acids as hydrophobic (H), positive (P), negative (N), or neutral (X) according to the charge of the amino acid, adding additional parameters to reduce the number of low energy conformations and allowing for more realistic protein simulations. Another model is the Crippen model which uses protein characteristics taken from crystal structures to inform the choice of native conformation.

According to the model, membrane proteins are in three classes based on how they are linked to the lipid bi-layer: # Integral proteins: Immersed in the bi-layer and held in place by the affinity of hydrophobic parts of the protein for the hydrophobic tails of phospholipids on interior of the layer. # Peripheral proteins: More hydrophilic, and thus are non-covalently linked to the polar heads of phospholipids and other hydrophilic parts of other membrane proteins on the surface of the membrane. # Lipid anchored proteins: Essentially hydrophilic, so, are also located on the surface of the membrane, and are covalently attached to lipid molecules embedded in the layer. As for the fluid nature of the membrane, the lipid components are capable of moving parallel to the membrane surface and are in constant motion.

The behavior of quantum dots (QDs) in solution and their interaction with other surfaces is of great importance to biological and industrial applications, such as optical displays, animal tagging, anti-counterfeiting dyes and paints, chemical sensing, and fluorescent tagging. However, unmodified quantum dots tend to be hydrophobic, which precludes their use in stable, water-based colloids. Furthermore, because the ratio of surface area to volume in a quantum dot is much higher than for larger particles, the thermodynamic free energy associated with dangling bonds on the surface is sufficient to impede the quantum confinement of excitons. Once solubilized by encapsulation in either a hydrophobic interior micelle or a hydrophilic exterior micelle, the QDs can be successfully introduced into an aqueous medium, in which they form an extended hydrogel network.

Those inhibitors that interact with the catalytic site occupy part of the active site, primarily around the Q pocket and occasionally close to the M pocket. A major point of interaction is a conserved hydrophobic pocket that is involved in orienting the substrate purine ring for interaction with a glutamine residue that is crucial for the catalytic mechanism of the PDEs. The interactions of inhibitors can be split into three major types: interactions with the metal ions mediated through water, H-bond interactions with the protein residues involved in nucleotide recognition and most importantly the interaction with the hydrophobic residues lining the cavity of the active site. All known inhibitors seem to exploit these three types of interactions and hence these interactions should guide the design of new types of inhibitors.

The membrane consists of many microcavities which allow the gas to escape, while its hydrophobicity characteristic prevents the liquid fuel from leaking through. More fuel flows in to replace the volume previously kept by the waste gas, and the reaction is allowed to continue. A well-known application of ultrahydrophobic surfaces is on heat exchangers, where they can improve droplet shedding and even cause jumping-droplet condensation, with potential for powerplants, heating and air conditioning, and desalination. Rare earth oxides, which are found to exhibit intrinsically hydrophobic surfaces, offer an alternative to surface coatings, allowing the development of thermally stable hydrophobic surfaces for heat exchangers operating at high temperature Ultrahydrophobic desalination membranes for membrane distillation have also been fabricated for improved fouling resistance, which can be fabricated effectively with chemical vapor deposition.

It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane. More recent research has demonstrated that no perturbation of Complex I occurs upon NDUFA4 deletion, calling into question its role in this complex. It has been demonstrated that NDUFA4 plays a role in Complex IV function and biogenesis, however, with some authors suggesting that the NDUFA4 gene be renamed and the structure of both Complex I and Complex IV be re-evaluated.

Hydrophobic silica is used to solve technical problems in a number of products including, but not limited to, paints, inks, adhesives, plastics, coatings, toners, defoamers, silicone rubber, sealants, cosmetics, food additives, polyester resins, cable gels, and greases. It's often manufactured as both single and multiphase composites in order to enhance properties such as dispersion, stability behavior, resistance to water, and functionality.

Myristoylation is thus a form of "molecular switch." Both hydrophobic myristoyl groups and "basic patches" (highly positive regions on the protein) characterize myristoyl-electrostatic switches. The basic patch allows for favorable electrostatic interactions to occur between the negatively charged phospholipid heads of the membrane and the positive surface of the associating protein. This allows tighter association and directed localization of proteins.

CP, like other fungal surface proteins, is able to self-assemble in vitro. CP is a 120 amino acid protein, containing 40% hydrophobic residues. It is one of the rare examples of protein in which contains a Hopf link. The link is formed by covalent loops - the pieces of protein backbone closed by two disulphide bonds (formed out of four cysteine residues).