中国生物工程杂志

Abstract: Disulfide bonds play an important role in stability of protein conformation and maintaining of protein activity. However, formation of natural disulfide bonds is a rate-limiting step in protein correct folding. With study on protein disulfide isomerase and folding intermediates, folding mechanism of disulfide-rich proteins has been clarified gradually. The protein folding mechanism is focused on in this review, which was understood by formation of disulfide bonds in vivo and protein oxidative folding in vitro, and its application in genetic engineering. These new findings may represent future directions for improving the quality of recombinant protein which is rich with disulfide bonds