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

doi:10.1002/anie.200500577

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

Department of Chemistry

Research output: Contribution to journal › Article › Research › peer-review

33 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 language	English
Pages (from-to)	4939-4944
Journal	Angewandte Chemie - International Edition
Volume	44
Issue number	31
DOIs	https://doi.org/10.1002/anie.200500577
Publication status	Published - 5 Aug 2005

Keywords

NMR spectroscopy
Protein engineering
Proteins
Ubiquitin

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10.1002/anie.200500577

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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. {\textcopyright} 2005 Wiley-VCH Verlag GmbH & Co. KGaA.",

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AU - Meldrum, Jill K.

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AU - Crespo, Maria D.

AU - Holmes, Elizabeth

AU - Searle, Mark S.

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KW - NMR spectroscopy

KW - Protein engineering

KW - Proteins

KW - Ubiquitin

U2 - 10.1002/anie.200500577

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ER -

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

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