Engineering enhanced protein stability through β-turn optimization: Insights for the design of stable peptide β-hairpin systems

Emma R. Simpson, Jill K. Meldrum, Roger Bofill, Maria D. Crespo, Elizabeth Holmes, Mark S. Searle

Research output: Contribution to journalArticleResearchpeer-review

30 Citations (Scopus)

Abstract

(Figure Presented) One good turn: β-Turns are an important component of protein structure and nucleation sites for β-hairpin folding. With ubiquitin as a "host" system (see structure), protein engineering methods have been used to determine the energetic contribution of type I' β-turns to the stability of proteins, with a view to optimizing the rational design of model peptide systems. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.
Original languageEnglish
Pages (from-to)4939-4944
JournalAngewandte Chemie - International Edition
Volume44
Issue number31
DOIs
Publication statusPublished - 5 Aug 2005

Keywords

  • NMR spectroscopy
  • Protein engineering
  • Proteins
  • Ubiquitin

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