Tymovirus Coat Protein
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Tymovirus Coat Protein
In molecular biology, the Tymovirus coat protein refers to the protein coat of a virus order (biology), order, named ''Tymovirales''. More specifically this protein signature is found only in coat proteins from the related tymoviruses. The coat protein (CP) is also known as the virion protein. The virus coat is composed of 180 copies of the coat protein arranged in an icosahedral shell. Function Fundamentally, the viral coat protein functions as protection for the genetic material inside the virus, and as an aid to infecting the host cell with virus DNA. Essentially, the coat protein (CP) is a link between the genetic material and infecting the host. Since the genetic material in the virus consists of RNA the coat protein contains RNA binding sites. Additionally, the coat protein contains conserved histadine amino acid residues which help the virus to spread. Structure There are three subunits named, A, B and C. It contains a beta-jelly roll motif which consists of 9 beta-strands. ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Virus
A virus is a submicroscopic infectious agent that replicates only inside the living cells of an organism. Viruses infect all life forms, from animals and plants to microorganisms, including bacteria and archaea. Since Dmitri Ivanovsky's 1892 article describing a non-bacterial pathogen infecting tobacco plants and the discovery of the tobacco mosaic virus by Martinus Beijerinck in 1898,Dimmock p. 4 more than 9,000 virus species have been described in detail of the millions of types of viruses in the environment. Viruses are found in almost every ecosystem on Earth and are the most numerous type of biological entity. The study of viruses is known as virology, a subspeciality of microbiology. When infected, a host cell is often forced to rapidly produce thousands of copies of the original virus. When not inside an infected cell or in the process of infecting a cell, viruses exist in the form of independent particles, or ''virions'', consisting of (i) the genetic material, i. ...
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Order (biology)
Order ( la, wikt:ordo#Latin, ordo) is one of the eight major hierarchical taxonomic ranks in Linnaean taxonomy. It is classified between Family_(biology), family and Class_(biology), class. In biological classification, the order is a taxonomic rank used in the classification of organisms and recognized by the nomenclature codes. An immediately higher rank, superorder, is sometimes added directly above order, with suborder directly beneath order. An order can also be defined as a group of related families. What does and does not belong to each order is determined by a taxonomist, as is whether a particular order should be recognized at all. Often there is no exact agreement, with different taxonomists each taking a different position. There are no hard rules that a taxonomist needs to follow in describing or recognizing an order. Some taxa are accepted almost universally, while others are recognized only rarely. The name of an order is usually written with a capital letter. Fo ...
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Icosahedral
In geometry, an icosahedron ( or ) is a polyhedron with 20 faces. The name comes and . The plural can be either "icosahedra" () or "icosahedrons". There are infinitely many non- similar shapes of icosahedra, some of them being more symmetrical than others. The best known is the (convex, non- stellated) regular icosahedron—one of the Platonic solids—whose faces are 20 equilateral triangles. Regular icosahedra There are two objects, one convex and one nonconvex, that can both be called regular icosahedra. Each has 30 edges and 20 equilateral triangle faces with five meeting at each of its twelve vertices. Both have icosahedral symmetry. The term "regular icosahedron" generally refers to the convex variety, while the nonconvex form is called a ''great icosahedron''. Convex regular icosahedron The convex regular icosahedron is usually referred to simply as the ''regular icosahedron'', one of the five regular Platonic solids, and is represented by its Schläfli symbol , co ...
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Histadine
Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also. It is encoded by the codons CAU and CAC. Histidine was first isolated by Albrecht Kossel and Sven Gustaf Hedin in 1896. It is also a precursor to histamine, a vital inflammatory agent in immune responses. The acyl radical is histidyl. Properties of the imidazole side chain The conjugate acid (protonated form) of the imidazole side chain in histidine has a p''K''a of approximately 6.0. Thus, below a pH of 6, the imidazole rin ...
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Protein Domains
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer after ...
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