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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.
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:
The two amino acid residues are linked through a peptide bond. As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This polymerization of amino acids is what creates proteins.
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.
The amino acid residues are always joined by peptide bonds. Protein, though used colloquially to refer to any polypeptide, refers to larger or fully functional forms and can consist of several polypeptide chains as well as single chains. Proteins can also be modified to include non-peptide components, such as saccharide chains and lipids.
[4] [5] The amide group is called a peptide bond when it is part of the main chain of a protein, and an isopeptide bond when it occurs in a side chain, as in asparagine and glutamine. It can be viewed as a derivative of a carboxylic acid ( R−C(=O)−OH ) with the hydroxyl group ( −OH ) replaced by an amine group ( −NR′R″ ); or ...
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 somewhat archaic. A peptidergic agent (or drug) is a chemical which functions to directly modulate the peptide systems in the body or brain. An example is opioidergics, which are neuropeptidergics.
N-and O-glycosylation in which carbohydrates are attached to the peptide are naturally occurring, where N-glycosylation occurs through the amine group of an asparagine residue to form an amide bond. O-glycosylation occurs via serine or threonine residues , where the oxygen atom on the side chain binds to the carbohydrate through an ether bond.