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