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Strategic Use of Non-Native Diselenide Bridges to Steer Oxidative Protein Folding

Authors


  • This study was supported by the ETH Zurich. N.M. thanks the Israel Science Foundation for a postdoctoral fellowship. We thank Kenneth Woycechowsky and Greg Bulaj for helpful discussions.

Abstract

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Targeted insertion of a non-native diselenide cross-link into a cysteine-rich protein can be exploited to direct the early stages of oxidative folding so as to avoid accumulation of unproductive intermediates that limit folding efficiency. This simple strategy could facilitate the production of many difficult-to-fold peptides and proteins.

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