Amino acids are connected together in a chain to form polypeptide. Does it happen with disulphide bonds?
Answers
disulfide bond, also called an S-S bond, or disulfide bridge, is a covalent bond derived from two thiol groups. In biochemistry, the terminology R-S-S-R connectivity is commonly used to describe the overall linkages. The most common way of creating this bond is by the oxidation of sulfhydryl groups. (2 RSH → RS-SR + 2 H+ + 2 e-) This process of oxidation can produce stable protein dimers, polymers, or complexes, in which the sulfide bonds can help in protein folding. The process mostly occurs with the thiol groups in cysteine. [1]
Formal depiction of disulfide bond formation as an oxidation.
Disulfide bonds can occur two ways: intramolecularly and intermolecularly. Intermolecular disulfide bonds occur between polypeptide chains while intramolecular disulfide bonds occur within a polypeptide chain and are usually responsible for stabilizing tertiary structures of proteins. On the other hand, intermolecular disulfide bonds are attributed to stabilizing quaternary protein structures.
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