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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.
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 ...
The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. [1] [2] Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which ...
However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:
Mechanism of peptide bond cleavage by chymotrypsin. Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. [1]: 84–6 It catalyzes the hydrolysis of peptide bonds in L-isomers of tyrosine, phenylalanine, and tryptophan.
This reactive intermediate is attacked by the peptide N-terminal amine, forming a peptide bond. Formation of the O-acylisourea proceeds fastest in non-polar solvents such as dichloromethane. [14] DIC is particularly useful for SPPS since as a liquid it is easily dispensed, and the urea byproduct is easily washed away.
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]
The characteristic color of a positive biuret test. 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.
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