Strategic use of non-native diselenide bridges to steer oxidative protein folding

Norman Metanis, Donald Hilvert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

73 Scopus citations

Abstract

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.

Original languageAmerican English
Pages (from-to)5585-5588
Number of pages4
JournalAngewandte Chemie - International Edition
Volume51
Issue number23
DOIs
StatePublished - 4 Jun 2012
Externally publishedYes

Keywords

  • diselenide bonds
  • disulfide bonds
  • oxidative folding
  • selenocysteine
  • thiol-disulfide exchange

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