Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond.

ABSTRACT: Oxidative protein folding involves the formation of disulfide bonds and the regeneration of native structure (N) from the fully reduced and unfolded protein (R). Oxidative protein folding studies have provided a wealth of information on underlying physico-chemical reactions by which disulfide-bond-containing proteins acquire their catalytically active form. Initially, we review key events underlying oxidative protein folding using bovine pancreatic ribonuclease A (RNase A), bovine pancreatic trypsin inhibitor (BPTI) and hen-egg white lysozyme (HEWL) as model disulfide bond-containing folders and discuss consequential outcomes with regard to their folding trajectories. We re-examine the findings from the same studies to underscore the importance of forming native disulfide bonds and generat

SUBMITTER: Narayan M 

PROVIDER: S-EPMC7697891 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature