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Engineering Enhanced Protein Stability through β-Turn Optimization: Insights for the Design of Stable Peptide β-Hairpin Systems

Authors

  • Emma R. Simpson,

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
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  • Jill K. Meldrum,

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
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  • Roger Bofill Dr.,

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
    2. Current address: Unitat de Química Inorgànica, Departament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra-Catalonia, Spain
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  • Maria D. Crespo Dr.,

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
    2. Current address: Biozentrum der Universitat Basel, Division of Biophysical Chemistry, Klingelbergstrasse 70, 4056 Basel, Switzerland
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  • Elizabeth Holmes,

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
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  • Mark S. Searle Prof.

    1. Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK, Fax: (+44) 115-951-3564
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  • This work was supported by the Engineering and Physical Sciences Research Council (EPSRC) of the UK (studentships to E.R.S. and J.K.M.), the EU Marie Curie Individual Research Fellowship Scheme (R.B.), and the University of Nottingham (M.D.C.). We thank Dr. H. Williams and Mr. S. Simpson for assistance with NMR spectroscopy and modeling studies.

Abstract

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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.

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