Protein di sulphide isomerase is involved in
High-Yield Explanation
Disulfide bonds between and within polypeptides stabilize teiary and quaternary structures. However, disulfide bond formation is nonspecific. Under oxidizing conditions, a given cysteine can form a disulfide bond with the --SH of any accessible cysteinyl residue. By catalyzing disulfide exchange, the rupture of an S--S bond and its reformation with a different paner cysteine, protein disulfide isomerase facilitates the formation of disulfide bonds that stabilize a protein&;s native conformationPeptidyl cis-trans isomerase, protein disulphide isomerase and chaperones are involved in protein folding