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In molecular biology, a RING (short for Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C 3 HC 4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).
For shear number in barrels, displacement is measured in units of amino acid residues. The determination of shear number requires the assumption that each amino acid in one strand of a beta sheet is adjacent to just one amino acid in the neighboring strand (this assumption may not hold if, for example, a beta bulge is present). [ 12 ]
The incorporation of these nonstandard amino acids is rare. For example, 25 human proteins include selenocysteine in their primary structure, [64] and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic moiety in their active sites. [65] Pyrrolysine and selenocysteine are encoded via variant codons.
An example of a superdomain is the protein tyrosine phosphatase–C2 domain pair in PTEN, tensin, auxilin and the membrane protein TPTE2. This superdomain is found in proteins in animals, plants and fungi. A key feature of the PTP-C2 superdomain is amino acid residue conservation in the domain interface.
The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...
Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...
The CC chemokine (or β-chemokine) proteins have two adjacent cysteines (amino acids), near their amino terminus. There have been at least 27 distinct members of this subgroup reported for mammals, called CC chemokine ligands -1 to -28; CCL10 is the same as CCL9. Chemokines of this subfamily usually contain four cysteines (C4-CC chemokines ...
The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent sidechains on one side of the sheet are hydrophobic, while many of those adjacent to each other on the alternate side of the sheet are polar or charged (hydrophilic), [22] which can be useful if the sheet is to form a ...
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