Protein folding drives disulfide formation.
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ABSTRACT:
SUBMITTER: Kosuri P
PROVIDER: S-EPMC3506382 | biostudies-literature | 2012 Nov
REPOSITORIES: biostudies-literature
Publications
Protein folding drives disulfide formation.
Kosuri Pallav P Alegre-Cebollada Jorge J Feng Jason J Kaplan Anna A Inglés-Prieto Alvaro A Badilla Carmen L CL Stockwell Brent R BR Sanchez-Ruiz Jose M JM Holmgren Arne A Fernández Julio M JM
Cell 20121101 4
PDI catalyzes the oxidative folding of disulfide-containing proteins. However, the sequence of reactions leading to a natively folded and oxidized protein remains unknown. Here we demonstrate a technique that enables independent measurements of disulfide formation and protein folding. We find that non-native disulfides are formed early in the folding pathway and can trigger misfolding. In contrast, a PDI domain favors native disulfides by catalyzing oxidation at a late stage of folding. We propo ...[more]
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