127 Sentences With "structural protein" | Random Sentence Generator

We also know that UVA light penetrates deeper into the skin than UVB, destroying a structural protein called collagen.

Collagen is the main structural protein in animals — humans included — and plays a vital role in tissues like bones, tendons, ligaments, cartilage and skin.

And we are trying to literally insert into the muscles of these children a significantly truncated but still functional version of that same structural protein to try to keep them alive and keep them healthy.

In fact, collagen is "the main structural protein that forms the connective tissue throughout our body, from skin to bones, muscles, tendons and ligaments," said Dr. Shari Marchbein, a board-certified dermatologist based in New York.

The key to accelerated daytime wound healing, the scientists found, was that skin cells moved more rapidly to repair the wound and there was also more collagen – the main structural protein in skin – deposited around the wound site.

The scales, they found, have a hard mineralized outer layer to resist penetration that is bound to a tough-but-flexible inner layer by collagen – the main structural protein in skin and other connective tissues in the body.

About 80 percent of the dermis is collagen, a structural protein that gives skin its strength and helps make it elastic, so it can stretch and bounce back, says Jules Lipoff, an assistant professor of dermatology at the University of Pennsylvania.

The first two carry instructions for the production of enzymes, while TCHH encodes for a protein that, when joined together with filaments of keratin—a structural protein found in hair, feathers, and even the stuff that makes up rhino horn—contribute to the shape of individual hair strands.

The viral genome encodes viral structural protein. Virions consist of 1 structural protein(s) (major species located in the capsid. Viral structural protein: Capsid protein has a molar mass of 59000–71000 Da; is the coat protein. Capsid protein has a molecular mass of minor 'soluble' 28–30 kDa.

The viral genome encodes viral structural protein. Virions consist of 1 viral structural protein (major species), or 2 Viral structural proteins (detected in Norwalk virus, amyelosis chronic stunt virus and porcine enteric calicivirus located in the capsid. Viral structural protein: Capsid protein has a molar mass of 58000–60000 Da; is the coat protein. Capsid protein has a molecular mass of minor 'soluble' 28–30 kDa.

Some of these viral nonstructural protein functions are replicon formation, immunomodulation, and transactivation of viral structural protein encoding genes.

RoXaN (Rotavirus 'X'-associated non-structural protein) also known as ZC3H7B (zinc finger CCCH-type containing 7B), is a protein that in humans is encoded by the ZC3H7B gene. RoXaN is a protein that contains tetratricopeptide repeat and leucine-aspartate repeat as well as zinc finger domains. This protein also interacts with the rotavirus non-structural protein NSP3.

MIF4GD also has been verified by two-hybrid bait-prey experiments to interact with NSP7ab, or Non-structural protein 7, of SARS-CoV.

RSU-1 has also been seen to act as a structural protein in integrin-mediated focal-adhesion complexes. It bind strongly to the protein PINCH.

Wittmann and Brigitte Wittmann-Liebold)Jockusch H. Stability and genetic variation of a structural protein. Naturwissenschaften. 1968 Nov;55(11):514-8. No abstract available.

A viral structural protein is a viral protein that is a structural component of the mature virus. Examples include the SARS coronavirus 3a and 7a accessory proteins.

The NSm protein is a non-structural protein (not present in mature virion) and is critical to cell-to-cell movement within plant cells (8). The NSs protein is also a non-structural protein and contributes to suppression of RNA silencing during plant infection. Glycoproteins (GN/GC) are necessary for successful thrips transmission. The N protein contributes to viral replication, and coats the genomic RNA within the virion.

However, as in the case of the CFA1 fimbriae, the structural protein itself can sometimes act as an adhesion if a portion of the protein extends into the ECM.

This virus has been classified as Penaeus stylirostris hamaparvovirus. The genome is 4.1 kilobases in length. There are three open reading frames in its genome:Rai P, Safeena MP, Karunasagar I, Karunasagar I (2011) Complete nucleic acid sequence of Penaeus stylirostris hamaparvovirus (PstDNV) from India. Virus Res 158(1-2):37-45 a left non structural protein (NS1) of 2001 base pairs (bp), a mid non structural protein (NS2) of 1092 bp and a right capsid protein of 990 bp.

One fivefold symmetry axis is shown center. The cap gene produces an additional, non-structural protein called the Assembly-Activating Protein (AAP). This protein is produced from ORF2 and is essential for the capsid-assembly process.

Fibroblasts contain the receptor for this growth factor. Thus the cell "thinks" it is producing a structural protein, but it creates a self-stimulatory growth signal. The cell divides rapidly and tumor forms. The tissue is often positive for CD34.

The RNA genome encodes at least four polypeptides: these are the non-structural protein and the read-through product which are involved in virus replication (RNA-dependent RNA polymerase, RdRp); the movement protein (MP) which is necessary for the virus to move between cells and the coat protein (CP). The read-through portion of the RdRp may be expressed as a separate protein in TMV. The virus is able to replicate without the movement or coat proteins, but the other two are essential. The non-structural protein has domains suggesting it is involved in RNA capping and the read-through product has a motif for an RNA polymerase.

The viruses of this subgenus, like other coronaviruses, have a lipid bilayer envelope in which the membrane (M), envelope (E) and spike (S) structural proteins are anchored. Unlike other coronaviruses, viruses in this subgenus also have an additional shorter spike- like structural protein called hemagglutinin esterase (HE).

HCV genome E2 is a viral structural protein found in the hepatitis C virus. It is present on the viral envelope and functions as a host receptor binding protein, mediating entry into host cells. It is a key target for the design of entry inhibitors and vaccine immunogens.

An example is chitin a very durable structural protein used in surgicalCampbell-Reece Biology sutures as well as durable varnishes but is common to many animals especially crustaceans and insects. But is also found in the African clawed frog (Xenopus laevis).Wagner et al., 1993 Wagner et al.

Influenza non-structural protein (NS1) is a homodimeric RNA-binding protein found in influenza virus that is required for viral replication. NS1 binds polyA tails of mRNA keeping them in the nucleus. NS1 inhibits pre-mRNA splicing by tightly binding to a specific stem-bulge of U6 snRNA.

NSP2, is a rotavirus nonstructural RNA-binding protein that accumulates in cytoplasmic inclusions (viroplasms) and is required for genome replication. NSP2 is closely associated in vivo with the viral replicase. The non- structural protein NSP5 plays a role in the structure of viroplasms mediated by its interaction with NSP2.

To avoid IFN production, the non structural protein (NS1) of influenza will interact with CCD domain of TRIM25 to block RIG-I ubiquitination. Some studies have shown that a deletion of the CCD domain of TRIM25 prevents the binding of NS1. Without this ubiquitination, there won’t be IFN production.

Both segments have an ambisense organization, coding for a structural protein in one sense and the non-structural proteins on the complementary strand. DNA1—the larger segment of 6.5 kb—encodes the capsid protein VP1 (128 kiloDaltons) on one strand and three non-structural proteins—NS1 of 14 kiloDaltons (kDa), NS2 of 37 kDa and NS3 of 55 kDa—on the complementary strand. DNA2—the smaller segment of 6 kb—encodes the capsid protein VP2 (133 kDa) on one strand and the non- structural protein NS4 (27 kDa) on the complementary strand. The open reading frame 4 is 3318 nucleotide in length and encodes a predicted 1105 amino acid protein which has a conserved DNA polymerase motif.

Immunofluorescence staining pattern of vimentin antibodies. Produced by incubating vimentin primary antibodies and FITC labelled secondary antibodies with HEp-20-10 cells. Vimentin is a structural protein that in humans is encoded by the VIM gene. Its name comes from the Latin vimentum which refers to an array of flexible rods.

The extracellular matrix of granulation tissue is created and modified by fibroblasts. Initially, it consists of a network of type-III collagen, a weaker form of the structural protein that can be produced rapidly. This is later replaced by the stronger, long-stranded type-I collagen, as evidenced in scar tissue.

Nodavirus endopeptidase (, Black Beetle virus endopeptidase, Flock House virus endopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-Ala- or -Asn-Phe- The enzyme is coded by several nodaviruses that are insect pathogens.

Ragworms' teeth are made of a very tough, yet lightweight material. Unlike bone and tooth enamel, this is not mineralised with calcium, but is formed by a histidine rich protein, with bound zinc ions.Broomell et al. (2008) Cutting Edge Structural Protein from the Jaws of Nereis virens Biomacromolecules, 9 (6), pp 1669–1677.

P22TSP is a homotrimeric structural protein consisting of 666 amino acids. It is noncovalently bound to the neck of the viral capsid. It has been crystallized in space group P213 and has one monomer in the asymmetric unit. The secondary structure of P22TSP is dominated by a parallel Beta helix comprising 13 complete turns.

Fibronectin is a protein that will bind to extracellular membrane proteins. This technique allows for measurements of cell stiffness and provides insights into the functioning of structural proteins. The schematic shown at right depicts the experimental setup devised by Bonakdar and Schilling, et al. (2015) for studying the structural protein plectin in mouse cells.

Replication cycle of phleboviruses. Phleboviruses are viruses with a negative-sense RNA genome consisting of three segments. The small segment (S) codes for the viral N protein and a non structural protein, NSs via an ambisense coding strategy. The medium-sized segment (M) codes for a precursor of the viral glycoproteins and non-structural components.

The RNA2 segment has two open reading frames (ORFs) that code for a capsid protein and a non-structural protein with unknown function. The virus is composed of two structural domains, a shell (S) and a protrusion (P) domain. The Orsay virus was discovered in 2011 in Caenorhabditis elegans nematodes in rotting fruit in Orsay, France.

The genome has been sequenced. There are three segments—large (L), medium (M) and small (S). Five proteins have been identified—an RNA dependent RNA polymerase (RdRp), a glycoprotein N (Gn), a glycoprotein C (Gc), a nuclear protein (NP) and a non structural protein (NSs). The L segment encodes the RNA polymerase with 2084 amino acid residues.

However, hypoxia-mediated HIF-1α responses are also linked to the regulation of mitochondrial dysfunction through the formation of excessive reactive oxygen species in mitochondria. Other pathways also influence adult muscle character. For example, physical force inside a muscle fiber may release the transcription factor serum response factor from the structural protein titin, leading to altered muscle growth.

Smoothelin is a protein that in humans is encoded by the SMTN gene. This gene encodes a structural protein that is found exclusively in contractile smooth muscle cells. It associates with stress fibers and constitutes part of the cytoskeleton. This gene is localized to chromosome 22q12.3, distal to the TUPLE1 locus and outside the DiGeorge syndrome deletion.

Gelatin is the aerator most often used in the production of marshmallows. It is made up of collagen, a structural protein derived from animal skin, connective tissue, and bones. Not only can it stabilize foams, like albumen, but when combined with water it forms a thermally-reversible gel. This means that gelatin can melt, then reset due to its sensitivity to temperature.

Tetraparvoviruses are small, non enveloped animal viruses with a single-stranded DNA genome between 4 and 6 kb in length. There are 2 open reading frames (ORF) present in the genome. ORF1 encodes the non-structural protein (NS1) and ORF2 encodes the viral capsid proteins (VP1/VP2). Inverted terminal repeats are present at the 5′ and 3′ ends of the genome.

Collagen is a structural protein, often referred to as “the steel of biological materials”. There are multiple types of collagen: Type I (comprising skin, tendons and ligaments, vasculature and organs, as well as teeth and bone); Type II (a component in cartilage); Type III (often found in reticular fibers); and others. Collagen has a hierarchical structure, forming triple helices, fibrils, and fibers.

Diagram showing the creation of alpha keratins helical structure. Keratin is a structural protein located at the hard surfaces in many vertebrates. Keratin has two forms, α-keratin and β-keratin, that are found in different classes of chordates. The naming convention for these keratins follows that for protein structures: alpha keratin is helical and beta keratin is sheet-like.

Chromosome 21 open reading frame 91 is a protein that in humans is encoded by the C21orf91 gene. EURL is a structural protein gene that is encoded within the human chromosome 21. It stands for gene Expressed in Undifferentiated Retina and Lens and was first found in chick embryos. It is also known as C21orf 91 (Chromosome 21 open reading frame 91).

The etiology of autism may include excessive glutamatergic mechanisms. In small studies, memantine has been shown to significantly improve language function and social behavior in children with autism. Research is underway on the effects of memantine in adults with autism spectrum disorders. A link between glutamate receptors and autism was also identified via the structural protein ProSAP1 SHANK2 and potentially ProSAP2 SHANK3.

This is due to IRAK4's function as both a structural protein and as a kinase. Both of these functions are required for the myddosome complex formation. Additionally, IRAK4 has been shown to be absolutely essential in a TLR signalling. IRAK4 deficient mice have a profoundly impaired ability to produce IL-6, TNF-α, and IL-12 in response to TLR ligands.

Branching morphogenesis over 2 days by Madin-Darby Canine Kidney cells in response to Hepatocyte Growth Factor (HGF). Images were acquired by fluorescence confocal microscopy, showing the structural protein actin, which highlights cell borders. Left: multicellular hollow spheres of cells, termed acini, were grown in 3D culture. Right: after 2 days of treatment with HGF cells have formed multiple branches.

The prefix osteo- indicates that the protein is expressed in bone, although it is also expressed in other tissues. The suffix -pontin is derived from "pons," the Latin word for bridge, and signifies osteopontin's role as a linking protein. Osteopontin is an extracellular structural protein and therefore an organic component of bone. Synonyms for this protein include sialoprotein I and 44K BPP (bone phosphoprotein).

FKBP14 is a gene which codes for a structural protein named FKBP prolyl isomerase 14. This protein is believed to aid in the process of procollagen folding and is located in the endoplasmic reticulum that functions to process and transport proteins. Procollagens are collagen precursors located in the extracellular matrix that give tissues elasticity, strength, and support. This gene is involved in patterning the collagen structure.

The microscopic "hairs" of these cells are structural protein filaments that project out into the fluid. The hair cells are mechanoreceptors that release a chemical neurotransmitter when stimulated. Sound waves moving through fluid flows against the receptor cells of the organ of Corti. The fluid pushes the filaments of individual cells; movement of the filaments causes receptor cells to become open to receive the potassium-rich endolymph.

The RNA genome is bound to capsid (C) proteins, which are 105 amino-acid residues long, to form the nucleocapsid. The capsid proteins are one of the first proteins created in an infected cell; the capsid protein is a structural protein whose main purpose is to package RNA into the developing viruses. The capsid has been found to prevent apoptosis by affecting the Akt pathway.

Replication of the coxsackie virus happens through contributions of the host and virus components. After cell entry of the virus and its internalization into the Golgi and endoplasmic reticulum and viral un-coating, viral RNA is released. Ribosomes on the rough endoplasmic reticulum translate the RNA into viral polyprotein. This polyprotein in processed into structural protein P1 and non-structural proteins P2 and P3.

A gene occurs in avian polyomaviruses in a similar genomic position and was originally annotated as an agnogene, but it has no detectable sequence similarity to the mammalian examples. The protein product of this gene has been detected in the capsids of mature virions, leading to its reclassification as VP4 to reflect its distinct role as a structural protein. However, it is still often referred to as "avian agnoprotein 1a".

A viral noncoding RNA of 140 nucleotides, named as bocavirus- encoded small RNA (BocaSR), is expressed from the 3' noncoding region after the VP ORF. NP1 is a small non-structural protein that could induce apoptosis in transfection of HeLa cells. There is a single promoter located within the 3' hairpin. This is responsible for, by alternative splicing and alternative polyadenylation, for the generation of several (at least 6) mRNAs.

Structure of Collagen I fibrils Collagen is the major structural protein outside cells in many connective tissues of animals. As the primary component of connective tissue, it has the largest amount among protein in mammals, occupying 25% to 35% of all protein content in the body. The fibrils in collagen are packed in a crimp structure. The stress/strain curve of collagen, such as tendon, can be subdivided into several regions.

Myelin P2 protein is a protein that in humans is encoded by the PMP2 gene. Myelin protein P2 is a constituent of peripheral nervous system (PNS) myelin, also present in small amounts in central nervous system (CNS) myelin. As a structural protein, P2 is thought to stabilize the myelin membranes, and may play a role in lipid transport in Schwann cells. Structurally, P2 belongs to the family of cytoplasmic fatty acid-binding proteins (FABPs).

Spinous cells serve “as a physical and biological barrier to the environment, preventing penetration by irritants and allergens and loss of water while maintaining internal homeostasis. They accomplish this in two ways. First, they are keratinocytes (keratin cells) whose primary function is to produce keratin, a strong structural protein. The keratin accumulates within each spinous cell as it moves upward through the epidermis layers, until the cell is almost completely filled with hardening keratin (keratinisation).

The S segment encodes two proteins: the nucleoprotein (N) and a non-structural protein (NSs) which inhibits transcription via inhibiting host cell RNA polymerase II resulting in decreased interferon (INF) induction. The M segment encodes a single polyprotein (M polyprotein) that is post-translationally processed into two surface glycoproteins (GNand GC) which are the targets of neutralizing antibodies, and a nonstructural protein, NSM. The L segment encodes a RNA- dependent RNA polymerase.

NF2 is caused by a defect in the gene that normally gives rise to a product called Merlin or Schwannomin, located on chromosome 22 band q11-13.1. Merlin was first discovered as a structural protein functioning as an actin cytoskeleton regulator. Later merlin's tumour suppressant role was described. Merlin regulates multiple proliferative signalling cascades such as receptor tyrosine kinase signalling, p21-activated kinase signalling, Ras signalling, MEK-ERK cascade, MST-YAP cascade.

The NS3 protein encodes a RNA triphosphatase within its helicase domain. It uses the helicase ATP hydrolysis site to remove the γ-phosphate from the 5′ end of the RNA. The N-terminal domain of the non-structural protein 5 (NS5) has both the N7-methyltransferase and guanylyltransferase activities necessary for forming mature RNA cap structures. RNA binding affinity is reduced by the presence of ATP or GTP and enhanced by S-adenosyl methionine.

In this case, the tendons (and associated muscles) are named for their most distal action (digital flexion). Tendons form in the embryo from fibroblasts which become more tightly packed as the tendon grows. As tendons develop they lay down collagen, which is the main structural protein of connective tissue. As tendons pass near bony prominences, they are protected by a fluid filled synovial structure, either a tendon sheath or a sac called a bursa.

Avulaviruses have a hemagglutinin-neuraminidase attachment protein and do not produce a non-structural protein C. Avulaviruses can be separated into distinct serotypes using hemagglutination assay and neuraminidase assay. All avulaviruses hemagglutinate chicken RBCs except for avian metaavulavirus 5 which does not hemagglutinate RBCs from any species. Avian metaavulavirus 6 is unique to the presence of the SH gene between the F and HN genes. Avian metaavulavirus 11 has the longest genome among the APMVs.

Elastin is a fibrous protein common in various soft tissues, like skin, blood vessels and lung tissue. Each monomer connects with each other, forming a 3D network, with ability to endure over 200% strain before deformation. Keratin is a structural protein mainly found in hair, nails, hooves, horns, quills. Basically keratin is formed by polypeptide chains, which coil into α-helices with sulfur cross-links or bond into β-sheets linked by hydrogen bonding.

The translation of the large ORF transcript produces a 114-kDa polyprotein. The mature VP4 protein, viral protease, assists this process to increase the processing of the polyprotein to generate preVP2 capsid protein, VP3 viral ribonucleoprotein (RNP), and additional VP4 proteins. In addition VP3 proteins can associate with pre-VP2 as a structural protein and with VP1 to function as a transcriptional activator. The small ORF of segment A consists of 711 nucleotides.

Alpha-keratin, or α-keratin, is a type of keratin found in vertebrates. This protein is the primary component in hairs, horns, mammalian claws, nails and the epidermis layer of the skin. α-keratin is a fibrous structural protein, meaning it is made up of amino acids that form a repeating secondary structure. The secondary structure of α-keratin is very similar to that of a traditional protein α-helix and forms a coiled coil.

GvpA is a gas vesicle structural protein found in different phyla of bacteria and archaea for example in Halobacterium salinarum or Haloferax mediterranei. Gas vesicles are small, hollow, gas filled protein structures found in several cyanobacterial and archaebacterial microorganisms. They allow the positioning of the bacteria at a favourable depth for growth. GvpA associates with GvpC, to build up gas vesicles, hollow protein structures which are used by planktonic organisms to perform vertical migration.

In molecular biology, VP40 is the name of a viral matrix protein. Most commonly it is found in the Ebola virus (EBOV), a type of non-segmented, negative-strand RNA virus. Ebola virus causes a severe and often fatal haemorrhagic fever in humans, known as Ebola virus disease. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells.

Production of protein kinase R, for example, can be disrupted in cells infected with JEV. Some viruses escape the anti-viral activities of interferons by gene (and thus protein) mutation. The H5N1 influenza virus, also known as bird flu, has resistance to interferon and other anti-viral cytokines that is attributed to a single amino acid change in its Non- Structural Protein 1 (NS1), although the precise mechanism of how this confers immunity is unclear.

In lipid transport, apolipoproteins function as structural components of lipoprotein particles, ligands for cell-surface receptors and lipid transport proteins, and cofactors for enzymes (e.g. apolipoprotein C-II for lipoprotein lipase and apolipoprotein A-I (apoA1) for lecithin-cholesterol acyltransferase). Different lipoproteins contain different classes of apolipoproteins, which influence their function. Apolipoprotein A-I (apoA1) is the major structural protein component of high-density lipoproteins (HDL), although it is present in other lipoproteins in smaller amounts.

Through the mechanisms of evolution, different species of bacteria have developed different solutions to the problem of attaching receptor specific proteins to the bacteria surface. Today many different types and subclasses of bacterial adhesins may be observed in the literature. The typical structure of a bacterial adhesion is that of a fimbria or pilus. The bacterial adhesion consists primarily of an intramembranous structural protein which provides a scaffold upon which several extracellular adhesins may be attached.

Like protease inhibitors, bevirimat and other maturation inhibitors interfere with protease processing of newly translated HIV polyprotein precursor, called gag. Gag is an essential structural protein of the HIV virus. Gag undergoes a chain of interactions both with itself and with other cellular and viral factors to accomplish the assembly of infectious virus particles. HIV assembly is a two-stage process involving an intermediate immature capsid that undergoes a structurally dramatic maturation to yield the infectious particle.

Noroviruses contain a linear, non-segmented, positive-sense RNA genome of approximately 7.5 kilobases, encoding a large polyprotein which is cleaved into six smaller non-structural proteins (NS1/2 to NS7) by the viral 3C-like protease (NS6), a major structural protein (VP1) of about 58~60 kDa and a minor capsid protein (VP2). The most variable region of the viral capsid is the P2 domain, which contains antigen-presenting sites and carbohydrate-receptor binding regions.

Duchenne muscular dystrophy is an X-linked genetic disorder that results in the absence of the structural protein dystrophin at the neuromuscular junction. It affects 1 in 3,600–6,000 males and frequently causes death by the age of 30. The absence of dystrophin causes muscle degeneration, and patients present with the following symptoms: abnormal gait, hypertrophy in the calf muscles, and elevated creatine kinase. If left untreated, patients may suffer from respiratory distress, which can lead to death.

If a third open reading frame is present (depends on the genus) it encodes a second non structural protein. The genome is anmbisense, encoding proteins on both the positive sense and negative sense directions. Transcriptional regulation and post-transcriptional modification are used to produce different nonstructural proteins and structural proteins. Virions enter the host cell is achieved by attachment to host receptors, which may be mediated by clathrin- mediated endocytosis or clathrin-independent dynamin-dependent endocytosis.

BFSP2 is a gene that encodes the protein phakinin ("beaded filament structural protein 2") in humans. More than 99% of the vertebrate ocular lens consists of terminally differentiated lens fiber cells. Two lens-specific intermediate filament proteins, the protein product of this gene (CP49 or phakinin) and filensin (also known as CP115), are expressed only after fiber cell differentiation has begun. Both proteins are found in a structurally unique cytoskeletal element that is referred to as the beaded filament (BF).

Tropocollagen molecule: three left-handed procollagens (red, green, blue) join to form a right-handed triple helical tropocollagen. Collagen () is the main structural protein in the extracellular matrix in the various connective tissues in the body. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix.

There was a sleep related increase in processes that involve the synthesis and maintenance of the synapse. Such processes include membrane trafficking, synaptic vesicle recycling, myelin structural protein formation, and cholesterol and protein synthesis. In a different study it was found that there was a sleep related increase in calmodulin-dependent protein kinase IV that has been specifically involved in synaptic depression and in the consolidation of long-term memory. These findings encourage an association between sleep and different aspects of neural plasticity.

After the unbound probes are washed away, the western blot is ready for detection of the probes that are labeled and bound to the protein of interest. In practical terms, not all westerns reveal protein only at one band in a membrane. Size approximations are taken by comparing the stained bands to that of the marker or ladder loaded during electrophoresis. The process is commonly repeated for a structural protein, such as actin or tubulin, that should not change between samples.

Fascin is a structural protein found in mesenchyme, nervous, and retinal tissue and is used in the bundling of actin molecules. The structure of human fascin has been determined to a resolution of 1.8 Å (PDBID 3LLP) and reveals an arrangement of four tandem beta-trefoil domains that form a two lobed structure with pseudo 2-fold symmetry. It is stabilized by a hydrophobic core and a hydrophilic surface since it is often found inside cell cytoplasm in the formation of filopodia.

BFSP1 is a gene that encodes the protein filensin ("beaded filament structural protein 1") in humans. More than 99% of the vertebrate ocular lens is made up of terminally differentiated lens fiber cells. Two lens-specific intermediate filament proteins, phakinin (also known as CP49) and the protein product of this gene, filensin (or CP115), are expressed only after fiber cell differentiation has begun. Both proteins are found in a structurally unique cytoskeletal element that is referred to as the beaded filament (BF).

Another important structural protein is the phosphoprotein N, which is responsible for the helical symmetry of the nucleocapsid that encloses the genomic RNA. Genetic recombination can occur when at least two viral genomes are present in the same infected host cell. RNA recombination appears to be a major driving force in coronavirus evolution. Recombination can determine genetic variability within a CoV species, the capability of a CoV species to jump from one host to another and, infrequently, the emergence of a novel CoV.

In anatomy, a crystallin is a water-soluble structural protein found in the lens and the cornea of the eye accounting for the transparency of the structure. It has also been identified in other places such as the heart, and in aggressive breast cancer tumors. Since it has been shown that lens injury may promote nerve regeneration, crystallin has been an area of neural research. So far, it has been demonstrated that crystallin β b2 (crybb2) may be a neurite-promoting factor.

Since it is a transcriptional factor, HOX B6 regulates erythpoigenesis (red blood cell formation) using mRNA as the basis for certain protein productions. The specific gene factor for erytopoigenesis has relatively been unobserved in the scientific community, and no known diseases have been associated with a defect HOX B6 gene. However, it has been shown in correlation with major skeletal deformations. HOXB6 is a structural protein that has been shown to influence the growth and differentiation of the different blood lineages.

Myotilin is a structural protein that, along with titin and alpha-actinin give structural integrity to sarcomeres at Z-discs in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells. A ternary complex myotilin/actin/alpha-actinin can be observed in vitro and actin bundles formed under these conditions appear more tightly packed than those induced by alpha-actinin alone. It was demonstrated that myotilin stabilizes F-actin by slowing down the disassembly rate.

The viral RNA is translated into a polyproteinss and then cleaved by viral and cellular proteases into the structural (C, prM, and E) and non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, 2K, NS4B, and NS5). Replication takes places on the surface of the endoplasmic reticulum within the membrane vessicles. A complementary negative sense RNA strand is formed via the RNA-dependent RNA polymerase (non- structural protein NS5) to create a double-stranded RNA. The dsRNA is transcribed producing viral mRNAs.

Basic units of chromatin structure Histone H2B is a structural protein that helps organize eukaryotic DNA. It plays an important role in the biology of the nucleus where it is involved in the packaging and maintaining of chromosomes, regulation of transcription, and replication and repair of DNA. Histone H2B helps regulate chromatin structure and function through post-translational modifications and specialized histone variants. Acetylation and ubiquitination are examples of two post- translational modifications that affect the function of histone H2B in particular ways.

The T = 13 shell of the IBDV capsid is formed by trimers of VP2, a protein generated by removal of the C-terminal domain from its precursor, pVP2. The trimming of pVP2 is performed on immature particles as part of the maturation process. The other major structural protein, VP3, is a multifunctional component lying under the T = 13 shell that influences the inherent structural polymorphism of pVP2. The virus-encoded RNA-dependent RNA polymerase, VP1, is incorporated into the capsid through its association with VP3.

The genome encodes several non- coding RNA structures; among them is the rubella virus 3' cis-acting element, which contains multiple stem-loops, one of which has been found to be essential for viral replication. The only significant region of homology between rubella and the alphaviruses is located at the NH2 terminus of non structural protein 3. This sequence has helicase and replicase activity. In the rubella genome these occur in the opposite orientation to that found in the alphaviruses indicating that a genome rearrangement has occurred.

Protein SvtR was the first crenarchaeal RHH regulator characterized in details and also the first viral coded transcriptional regulators within the Archaeal domain. It strongly represses the transcription of the minor structural protein and, to a lesser extent, of its own gene. The structure is very similar to that of bacterial RHH proteins despite the low sequence similarity, such as CopG, a bacterial plasmid copy number control regulator. A Sulfolobus islandicus coded transcription activator, Sta1, has also been shown to activate transcription of several viral genes.

NS2-3 protease (of hepatitis C virus, HCV) is an enzyme responsible for proteolytic cleavage between NS2 and NS3, which are non-structural proteins that form part of the HCV virus particle. NS3 protease of hepatitis C virus, on the other hand, is responsible for the cleavage of non-structural protein downstream. Both of these proteases are directly involved in HCV genome replication, that is, during the viral life-cycle that leads to virus multiplication in the host that has been infected by the virus.

Firstly the outer membrane is removed as the particle enters the cell; secondly the virus particle (without the outer membrane) fuses with the cellular membrane to release the core into the cytoplasm. The pox viral genes are expressed in two phases. The early genes encode the non-structural protein, including proteins necessary for replication of the viral genome, and are expressed before the genome is replicated. The late genes are expressed after the genome has been replicated and encode the structural proteins to make the virus particle.

To discourage seed predators, pulses contain trypsin inhibitors that interfere with digestion. Animals and plants have evolved to synthesise a vast array of poisonous products including secondary metabolites, peptides and proteins that can act as inhibitors. Natural toxins are usually small organic molecules and are so diverse that there are probably natural inhibitors for most metabolic processes. The metabolic processes targeted by natural poisons encompass more than enzymes in metabolic pathways and can also include the inhibition of receptor, channel and structural protein functions in a cell.

By the end of the 1940s Szent-Györgyi's team had postulated with evidence that contraction of actomyosin was equivalent to muscle contraction as a whole. But the notion was generally opposed, even from the likes of Nobel laureates such as Otto Fritz Meyerhof and Archibald Hill, who adhered to the prevailing dogma that myosin was a structural protein and not a functional enzyme. However, in one of his last contributions to muscle research, Szent-Györgyi demonstrated that actomyosin driven by ATP was the basic principle of muscle contraction.

The alphaviruses are small, spherical, enveloped viruses with a genome of a single strand of positive-sense RNA. The total genome length ranges between 11,000 and 12,000 nucleotides, and has a 5’ cap and a 3’ poly-A tail. The four non-structural protein genes are encoded in the 5′ two-thirds of the genome, while the three structural proteins are translated from a subgenomic mRNA colinear with the 3′ one-third of the genome. There are two open reading frames (ORFs) in the genome, nonstructural and structural.

Patients also don't have appropriate DNA repair, and they also have increased genomic instability. In normal conditions, the LMNA gene codes for a structural protein called prelamin A, which undergoes a series of processing steps before attaining its final form, called lamin A.LMNA Genes Genetics Home Reference Prelamin A contains a “CAAX”where C is a cysteine, an aliphatic amino acid, and X any amino acid. This motif at the carboxyl-termini of proteins triggers three sequential enzymatic modifications. First, protein farnesyltransferase catalyzes the addition of a farnesyl moiety to the cysteine.

Prolidase deficiency (PD) is an extremely uncommon autosomal recessive disorder associated with collagen metabolism that affects connective tissues and thus a diverse array of organ systems more broadly, though it is extremely inconsistent in its expression. Collagen is a structural protein found i.a. in bone, skin and connective tissues that is broken down into iminodipeptides at the end of its lifecycle. Of these dipeptides, those containing C-terminal proline or hydroxyproline would normally be broken down further by the enzyme Prolidase, recovering and thus recycling the constituent amino acids.

Keratin (high molecular weight) in bile duct cell and oval cells of horse liver. Fibrous keratin molecules supercoil to form a very stable, left-handed superhelical motif to multimerise, forming filaments consisting of multiple copies of the keratin monomer. The major force that keeps the coiled-coil structure is hydrophobic interactions between apolar residues along the keratins helical segments. Limited interior space is the reason why the triple helix of the (unrelated) structural protein collagen, found in skin, cartilage and bone, likewise has a high percentage of glycine.

A risk for myopia may be inherited from one's parents. Genetic linkage studies have identified 18 possible loci on 15 different chromosomes that are associated with myopia, but none of these loci is part of the candidate genes that cause myopia. Instead of a simple one-gene locus controlling the onset of myopia, a complex interaction of many mutated proteins acting in concert may be the cause. Instead of myopia being caused by a defect in a structural protein, defects in the control of these structural proteins might be the actual cause of myopia.

Several species colonize plants, animals, or other fungi as parasites or mutualistic symbionts and derive all their metabolic energy in form of nutrients from the tissues of their hosts. Owing to their long evolutionary history, the Ascomycota have evolved the capacity to break down almost every organic substance. Unlike most organisms, they are able to use their own enzymes to digest plant biopolymers such as cellulose or lignin. Collagen, an abundant structural protein in animals, and keratin—a protein that forms hair and nails—, can also serve as food sources.

A matricellular protein is a dynamically expressed non-structural protein that is present in the extracellular matrix (ECM). Rather than serving as stable structural elements in the ECM, these proteins are rapidly turned over and have regulatory roles. They characteristically contain binding sites for ECM structural proteins and cell surface receptors, and may sequester and modulate activities of specific growth factors. Examples of matricellular proteins include the CCN family of proteins (also known as CCN intercellular signaling protein), fibulins, osteopontin, periostin, SPARC family members, tenascin(s), and thrombospondins.

However, subsequent evidence such as the relatively common finding of variants in the gene in those without long QT syndrome, and the general need for a second stressor such as hypokalaemia to be present to reveal the QT prolongation, has suggested that this gene instead represents a modifier to susceptibility to QT prolongation. Some therefore dispute whether variants in KCNE2 are sufficient to cause Romano-Ward syndrome by themselves. LQT9 is caused by variants in the membrane structural protein, caveolin-3. Caveolins form specific membrane domains called caveolae in which voltage-gated sodium channels sit.

The envelope of the virus in electron micrographs appears as a distinct pair of electron-dense shells (shells that are relatively opaque to the electron beam used to scan the virus particle). The M protein is the main structural protein of the envelope that provides the overall shape and is a type III membrane protein. It consists of 218 to 263 amino acid residues and forms a layer of 7.8 nm thickness. It has three domains such as a short N-terminal ectodomain, a triple-spanning transmembrane domain, and a C-terminal endodomain.

GFP. This image was captured using confocal laser scanning microscopy Successful infection of a plant by a plant virus depends on its ability to move from the cell initially infected to neighbouring cells in order to spread infection. Unlike animal cells, plant cells have robust cell walls, which viruses cannot easily penetrate. A movement protein is a non- structural protein which is encoded by some plant viruses to allow their movement from one infected cell to neighbouring cells. Many, if not all, plant viruses encode a movement protein, and some express more than one.

Histone tails and their function in chromatin formation Histone H2B is a lightweight structural protein made of 126 amino acids. Many of these amino acids have a positive charge at cellular pH, which allows them to interact with the negatively charged phosphate groups in DNA. Along with a central globular domain, histone H2B has two flexible histone tails that extend outwards – one at the N-terminal end and one at C-terminal end. These are highly involved in condensing chromatin from the beads-on-a- string conformation to a 30-nm fiber.

In the case of HHblits, such matches are done on the level of HMM-HMM profiles, which grants additional sensitivity. Its prefiltering reduces the tens of millions HMMs to match against to a few thousands of them, thus speeding up the slow HMM-HMM comparison process. The HH-suite comes with a number of pre-built profile HMMs that can be searched using HHblits and HHsearch, among them a clustered version of the UniProt database, of the Protein Data Bank of proteins with known structures, of Pfam protein family alignments, of SCOP structural protein domains, and many more.

The Roussy–Lévy syndrome has been associated with two genetic mutations: a duplication of the PMP22 gene that carries the instructions for producing the peripheral myelin protein 22, a critical component of the myelin sheath; and a missense mutation in the MPZ gene which codes for myelin protein zero, a major structural protein of peripheral myelin. As PMP22 mutations are also associated with Charcot–Marie–Tooth disease type 1A and MPZ mutations are associated with Charcot–Marie–Tooth disease type 1B, it remains the subject of discussion whether the Roussy–Lévy syndrome is a separate entity or a specific phenotype of either disorder.

The way this system operates was shown in animal model that have a mutant rhodopsin gene. The injected AAV-ribozymes were optimized in vitro and used to cleave the mutant mRNA transcript of P23H (where most mutation occur) in vivo. Another mutation in the rhodopsin structural protein, specifically peripherin 2 which is a membrane glycoprotein involved in the formation of photoreceptor outersegment disk, can lead to recessive RP and macular degeneration in human (19). In a mouse experiment, AAV2 carrying a wild-type peripherin 2 gene driven by a rhodopsin promoter was delivered to the mice by subretinal injection.

A proposed classification scheme sorts viroporins into four classes based on their topology and orientation in the membrane. Class I viroporins possess a single transmembrane helix; in class IA the C-terminus is oriented into the cytosol and in class IB the N-terminus is so oriented. Class II viroporins possess a helix-turn-helix motif with both helices crossing the membrane; in class IIA both termini are oriented externally (extracellularly or toward the lumen of the endoplasmic reticulum) and in class IIB the termini are oriented toward the cytosol. Likely exceptions to this scheme exist, such as the rotavirus protein non-structural protein 4.

Banga's initial work as Szent-Györgyi's associate involved studying carbohydrate metabolism. She developed methods for the large-scale purification of ascorbic acid (vitamin C) from Hungarian paprika – work that entailed extracting the vitamin from close to a metric ton of paprika. After winning the Nobel Prize in Physiology or Medicine in 1937 (for work to which Banga contributed), Albert Szent-Györgyi switched his lab's focus to researching muscle contraction, motivated by the findings of Engelhardt and Ljubimova that the muscle protein myosin wasn't merely a structural protein – it had phosphatase (ATPase) activity. Banga confirmed these findings and further characterized myosin's ability to split ATP.

This kind of regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin. Collagen is not only a structural protein. Due to its key role in the determination of cell phenotype, cell adhesion, tissue regulation, and infrastructure, many sections of its non-proline-rich regions have cell or matrix association/regulation roles. The relatively high content of proline and hydroxyproline rings, with their geometrically constrained carboxyl and (secondary) amino groups, along with the rich abundance of glycine, accounts for the tendency of the individual polypeptide strands to form left-handed helices spontaneously, without any intrachain hydrogen bonding.

279x279px Non-structural protein 5B (NS5B) inhibitors are a class of direct acting antivirals widely used in the treatment of chronic hepatitis C. Depending on site of action and chemical composition, NS5B inhibitors may be categorized into three classes – nucleoside active site inhibitors (NIs), non nucleoside allosteric inhibitors, and pyrophosphate analogues. Subsequently, all three classes are then subclassified. All inhibit RNA synthesis by NS5B but at different stages/sites resulting in inability of viral RNA replication. Expression of direct acting NS5B inhibitors does not takes place cells that are not infected by hepatitis C virus, which seems to be beneficial for this class of drugs.

Hepatitis C is one of the most significant diseases to affect humans but despite its global impact, there are no vaccines or effective therapies without major side effects. The hepatitis C virus non-structural protein 5B (NS5B) has become a target of choice for the development of anti-hepatitis C virus drugs, as it is not expressed in cells that are not infected by heaptitis C virus. The treatment for patients with chronic hepatitis C that was used prior to the development of direct acting antivirals was ribavirin plus pegylated interferon alfa-2a. This treatment was dissatisfactory in many cases, both for the lack of efficacy and because of side effects.

Thus, many viruses (including HIV-1) are categorized as having a polycistronic genome, meaning they employ multiple active ORF's in a single gene. The HIV-1 virus requires a programmed -1 ribosomal frameshift signal (the HIV-1 Ribosomal Frameshift Signal) for the expression of the Pol gene, which is an example of a cis-acting element of gene regulation. In HIV-1, the gag ORF that encodes the 55 kDa Gag protein, the major viral structural protein, is located at the 5' end of the full-length viral mRNA. Translation of the 160 kDa Gag-Pol polyprotein is contingent on a -1 ribosomal frameshift event revealing the pol ORF.

The exact constitution of the ZFNs that are to be used to treat HIV is still unknown. The binding of ZFNs for the alteration of the Zif268 genelink, however, has been well-studied and is outlined below to illustrate the mechanism by which the zinc finger domain of ZFNs bind to DNA. The amino terminus of the alpha helix portion of zinc fingers targets the major grooves of the DNA helix and binds near the CCR5 gene positioning FokI in a suitable location for DNA cleavage. Zinc fingers are repeated structural protein motifs with DNA recognition function that fit in the major grooves of DNA.

Genome and polyprotein of members of the genus Flavivirus Members of the family Flaviviridae have monopartite, linear, single-stranded RNA genomes of positive polarity, 9.6 to 12.3 kilobase. The 5'-termini of flaviviruses carry a methylated nucleotide cap, while other members of this family are uncapped and encode an internal ribosome entry site. The genome encodes a single polyprotein with multiple transmembrane domains that is cleaved, by both host and viral proteases, into structural and non-structural proteins. Among the non-structural protein products (NS), the locations and sequences of NS3 and NS5, which contain motifs essential for polyprotein processing and RNA replication respectively, are relatively well conserved across the family and may be useful for phylogenetic analysis.

Like all noroviruses, MNV has linear, non-segmented, positive-sense RNA genome of approximately 7.5 kbp, encoding a large polyprotein which is cleaved into six smaller non-structural proteins (NS1/2 to NS7) by the viral 3C-like protease (NS6), a major structural protein (VP1) of about 58~60 kDa and a minor capsid protein (VP2). In addition to these proteins, MNV is unique amongst the noroviruses in possessing an additional fourth open reading frame overlapping the VP1 coding sequence. This additional reading frame encodes a virulence factor (VF1) which regulates the innate immune response. The 3'UTR of the viral genome forms stem-loop structures which have a role in virulence.

Marfanoid–progeroid–lipodystrophy syndrome (MPL), also known as Marfan lipodystrophy syndrome (MFLS) or progeroid fibrillinopathy, is an extremely rare medical condition which manifests as a variety of symptoms including those usually associated with Marfan syndrome, an appearance resembling that seen in neonatal progeroid syndrome (NPS; also known as Wiedemann–Rautenstrauch syndrome), and severe partial lipodystrophy. It is a genetic condition that is caused by mutations in the FBN1 gene, which encodes profibrillin, and affects the cleavage products of profibrillin, fibrillin-1, a fibrous structural protein, and asprosin, a glucogenic protein hormone. As of 2016, fewer than 10 cases of the condition have been reported. Lizzie Velásquez and Abby Solomon have become known publicly through the media for having the condition.

Comprehensive analysis of bidnavirus genes has shown that these viruses have evolved from a parvovirus ancestor from which they inherit a jelly-roll capsid protein and a superfamily 3 helicase. It has been further suggested that the key event that led to the separation of the bidnaviruses from parvoviruses was the acquisition of the PolB gene. A likely scenario has been proposed under which the ancestral parvovirus genome was integrated into a large virus- derived DNA transposon of the Polinton/Maverick family (polintoviruses) resulting in the acquisition of the polintovirus PolB gene along with terminal inverted repeats. Bidnavirus genes for a minor structural protein (putative receptor-binding protein) and a potential novel antiviral defense modulator were derived from dsRNA viruses (Reoviridae) and dsDNA viruses (Baculoviridae), respectively.

MVM uses two transcriptional promoters at map units (mu) 4 and 38 (p4 and p38) and a single polyadenylation site at mu 95 to create 3 major size classes of mRNAs, referred to as R1, R2 and R3, all of which have a short intron sequence between 46–48 mu removed. R1 is produced from p4 and is translated into non- structural protein 1 (NS1). However, in some P4 transcripts a second intron between 10–40 mu is also excised, creating R2 mRNAs that encode NS2 proteins of ~25 kDa. These share 85 amino acids of N-terminal sequence with NS1, and then splice into an alternate reading frame before finally reaching the short central intron where 2 different C-terminal hexapeptides can be added.

The major non-structural protein, NS1, is a site- and strand-specific endonuclease belonging to the HuH protein superfamily, and also carries a AAA+ SF3 helicase domain. NS1 initiates and drives the viral “rolling hairpin” replication mechanism (RHR), which is a linear adaptation of the more-common “rolling-circle” replication strategy used by many small circular prokaryotic and viral replicons. RHR is a unidirectional mechanism that displaces a single, continuous DNA strand, which rapidly folds and refolds to generate a series of concatemeric duplex replication intermediates. Unit length genomes are then excised from these intermediates by the NS1 endonuclease (reviewed in references 5 and 6), and packaged 3’-to-5’ into preformed empty capsids driven by the SF3 helicase activity of NS1/Rep.

An amber mutant of phage T4 contains a mutation that changes a codon for an amino acid in a protein to the nonsense stop codon TAG (see stop codon and nonsense mutation). If, upon infection, an amber mutant defective in a gene encoding a needed structural component of phage T4 is weakly suppressed (in an E. coli host containing a specific altered tRNA – see nonsense suppressor), it will produce a reduced number of the needed structural component. As a consequence few if any viable phage are formed. However, it was found that viable phage could sometimes be produced in the host with the weak nonsense suppressor if a second amber mutation in a gene that encodes another structural protein is also present in the phage genome.

Different strains of FCV can vary in virulence (the degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host). Being an RNA virus, FCV has a high elasticity of its genome, which makes it more adaptable to environmental pressures. This not only makes the development of vaccines more difficult, but also allows for the development of more virulent strains. In persistently infected cats, the gene for the major structural protein of the viral capsid (the outer protein coat of a mature virus) has been shown to evolve through immune-mediated positive selection, which allows the virus to escape detection by the immune system.

However, in some individuals with PCD, mutations thought to be in the gene coding for the key structural protein left-right dynein (lrd) result in monocilia which do not rotate. There is therefore no flow generated in the node, Shh moves at random within it, and 50% of those affected develop situs inversus, which can occur with or without dextrocardia, where the laterality of the internal organs is the mirror-image of normal. Affected individuals therefore have Kartagener syndrome. This is not the case with some PCD-related genetic mutations: at least 6% of the PCD population have a condition called situs ambiguus or heterotaxy, where organ placement or development is neither typical (situs solitus) nor totally reversed (situs inversus totalis) but is a hybrid of the two.

These are made of a viral envelope containing the glycoproteins hemagglutinin and neuraminidase wrapped around a central core. The central core contains the viral RNA genome and other viral proteins that package and protect this RNA. RNA tends to be single stranded but in special cases it is double. Unusually for a virus, its genome is not a single piece of nucleic acid; instead, it contains seven or eight pieces of segmented negative-sense RNA, each piece of RNA containing either one or two genes, which code for a gene product (protein). For example, the influenza A genome contains 11 genes on eight pieces of RNA, encoding for 11 proteins: hemagglutinin (HA), neuraminidase (NA), nucleoprotein (NP), M1 (matrix 1 protein), M2, NS1 (non-structural protein 1), NS2 (other name is NEP, nuclear export protein), PA, PB1 (polymerase basic 1), PB1-F2 and PB2.

TEM micrograph showing dengue virus virions (the cluster of dark dots near the center) Dengue fever virus (DENV) is an RNA virus of the family Flaviviridae; genus Flavivirus. Other members of the same genus include yellow fever virus, West Nile virus, Zika virus, St. Louis encephalitis virus, Japanese encephalitis virus, tick-borne encephalitis virus, Kyasanur forest disease virus, and Omsk hemorrhagic fever virus. Most are transmitted by arthropods (mosquitos or ticks), and are therefore also referred to as arboviruses (arthropod-borne viruses). The dengue virus genome (genetic material) contains about 11,000 nucleotide bases, which code for the three different types of protein molecules (C, prM and E) that form the virus particle and seven other non-structural protein molecules (NS1, NS2a, NS2b, NS3, NS4a, NS4b, NS5) that are found in infected host cells only and are required for replication of the virus.

His key contributions lie in the field of deformation and failure of structural protein materials such as collagen and silk, where his work revealed universal material design paradigms that enable protein materials to provide enhanced and diverse functionality despite limited resources (energy, material volume, weak building blocks such as H-bonds, etc.), and demonstrated how these mechanisms break down under extreme conditions and disease (impact, trauma, mutations, flaws, etc.). The impact of his work has been the establishment of the universality-diversity paradigm, explaining how multifunctionality (diversity) of material properties in biology is achieved by changing structural arrangements of few (universal) constituents rather than inventing new building blocks, or through reliance of the quality of building blocks. Some of Buehler's current work involves the use of ologs, a category-theoretic framework for knowledge representation, to encode the structure-function relationships inherent in hierarchical materials. Buehler has published more than 300 articles on theoretical and computational modeling of materials using various types of simulation methods, a monograph on atomistic modeling, a book on Biomateriomics, several book chapters, and has given hundreds of invited lectures, keynote talks and plenary speeches.