Harnessing selenocysteine reactivity for oxidative protein folding.

ABSTRACT: Although oxidative folding of disulfide-rich proteins is often sluggish, this process can be significantly enhanced by targeted replacement of cysteines with selenocysteines. In this study, we examined the effects of a selenosulfide and native versus nonnative diselenides on the folding rates and mechanism of bovine pancreatic trypsin inhibitor. Our results show that such sulfur-to-selenium substitutions alter the distribution of key folding intermediates and enhance their rates of interconversion in a context-dependent manner.

SUBMITTER: Metanis N 

PROVIDER: S-EPMC5514408 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature