Premium
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.