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

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

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

Author(s) -

Simpson Emma R.,

Meldrum Jill K.,

Bofill Roger,

Crespo Maria D.,

Holmes Elizabeth,

Searle Mark S.

Publication year - 2005

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200500577

Subject(s) - rational design , protein engineering , protein folding , peptide , turn (biochemistry) , folding (dsp implementation) , protein design , stability (learning theory) , component (thermodynamics) , protein structure , chemistry , biological system , nanotechnology , computer science , materials science , physics , engineering , biology , biochemistry , mechanical engineering , enzyme , thermodynamics , machine learning

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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