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

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Resum

(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.
Idioma originalAnglès
Pàgines (de-a)4939-4944
RevistaAngewandte Chemie - International Edition
Volum44
Número31
DOIs
Estat de la publicacióPublicada - 5 d’ag. 2005

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