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 Aug. 2014
Accepted
22 Sept. 2014
First published
23 Sept. 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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