Issue 1, 2015

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.

Graphical abstract: Harnessing selenocysteine reactivity for oxidative protein folding

Supplementary files

Article information

Article type
Edge Article
Submitted
06 8 2014
Accepted
22 9 2014
First published
23 9 2014
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2015,6, 322-325

Author version available

Harnessing selenocysteine reactivity for oxidative protein folding

N. Metanis and D. Hilvert, Chem. Sci., 2015, 6, 322 DOI: 10.1039/C4SC02379J

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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