
Open access
Date
2015-01-01Type
- Journal Article
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. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000094087Publication status
publishedExternal links
Journal / series
Chemical ScienceVolume
Pages / Article No.
Publisher
Royal Society of ChemistryOrganisational unit
03492 - Hilvert, Donald (emeritus) / Hilvert, Donald (emeritus)
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