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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.
Chemical ligation of unprotected peptides is enabled by formation of an unnatural moiety, i.e. non-peptide bond, linking the two peptide segments in the ligation product. It was envisioned as a general method that would greatly simplify the chemical synthesis of protein molecules and enable the application of the entire repertoire of chemistry ...
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 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.
In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of ...
In native chemical ligation, the ionized thiol group of an N-terminal cysteine residue of an unprotected peptide attacks the C-terminal thioester of a second unprotected peptide, in an aqueous buffer at pH 7.0 and room temperature. This transthioesterification step is reversible in the presence of an aryl thiol catalyst, rendering the reaction ...
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.