- Journal Article
Rights / licenseCreative Commons Attribution 3.0 Unported
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. Show more
Journal / seriesChemical Science
Pages / Article No.
PublisherRoyal Society of Chemistry
Organisational unit03492 - Hilvert, Donald / Hilvert, Donald
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