Protein di sulphide isomerase is involved in
Protein synthesis
Protein degradation
Protein folding
Protein quaernary structure formation
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
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