Harnessing selenocysteine reactivity for oxidative protein folding

Norman Metanis, Donald Hilvert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

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.

Original languageAmerican English
Pages (from-to)322-325
Number of pages4
JournalChemical Science
Volume6
Issue number1
DOIs
StatePublished - 1 Jan 2015

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