Journal
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY
Volume 24, Issue -, Pages 211-235Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.cellbio.24.110707.175333
Keywords
thiol-disulfide exchange; oxidative folding; RNAse A; BPTI; hirudin; oxidoreductase
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
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Determining the mechanism by which proteins attain their native structure is an important but difficult problem in basic biology. The study of protein folding is difficult because it involves the identification and characterization of folding intermediates that are only very transiently present. Disulfide bond formation is thermodynamically linked to protein folding. The bioavailability of thiol trapping reagents and the relatively slow kinetics of disulfide bond formation have facilitated the isolation, purification, and characterization of disulfide-linked folding intermediates. As a result, the folding pathways of several disulfide-rich proteins are among the best known of any protein. This review discusses disulfide bond formation and its relationship to protein folding in vitro and in vivo.
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