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Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
The resulting peptides are called W>F "substitutants". Such W>F substitutants are abundant in certain cancer types and have been associated with increased IDO1 expression. Functionally, W>F substitutants can impair protein activity. [12]
In biochemistry, the Corey-Pauling rules are a set of three basic statements that govern the secondary nature of proteins, in particular, the CO-NH peptide link. They were originally proposed by Robert Corey and Linus Pauling. [1] The rules are as follows: The atoms in a peptide link all lie on the same plane.
A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome.
The ribosomes catalyze the formation of covalent peptide bonds between the encoded amino acids to form a polypeptide chain. [citation needed] Following translation the polypeptide chain must fold to form a functional protein; for example, to function as an enzyme the polypeptide chain must fold correctly to produce a functional active site.
The peptidyl transferase center (EC 2.3.2.12) is an aminoacyltransferase ribozyme (RNA enzyme) located in the large subunit of the ribosome.It forms peptide bonds between adjacent amino acids during the translation process of protein biosynthesis. [1]
A neuropeptide is a peptide that is active in association with neural tissue. A lipopeptide is a peptide that has a lipid connected to it, and pepducins are lipopeptides that interact with GPCRs. A peptide hormone is a peptide that acts as a hormone. A proteose is a mixture of peptides produced by the hydrolysis of proteins. The term is ...
In chemistry, the biuret test (IPA: / ˌ b aɪ j ə ˈ r ɛ t /, / ˈ b aɪ j ə ˌ r ɛ t / [1]), also known as Piotrowski's test, is a chemical test used for detecting the presence of at least two peptide bonds in a molecule. In the presence of peptides, a copper(II) ion forms mauve-colored coordination complexes in an alkaline solution.