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Incremental Contribution to Protein Stability from a β Hairpin “Finger”: Limits on the Stability of Designed β Hairpin Peptides
Author(s) -
Searle Mark S.,
Platt Geoffrey W.,
Bofill Roger,
Simpson Stephen A.,
Ciani Barbara
Publication year - 2004
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.200352955
Subject(s) - stability (learning theory) , protein folding , limit (mathematics) , ubiquitin , sequence (biology) , protein stability , folding (dsp implementation) , chemistry , physics , computer science , mathematics , biochemistry , engineering , mathematical analysis , machine learning , electrical engineering , gene
Back to the fold : A new method to determining the stability of a β hairpin is described. A β hairpin forming sequence (β4) is introduced into native ubiquitin (see structure) enabling the contribution to protein stability of this structural motif to be estimated. This data provides both an upper limit on stability for autonomously folding β hairpins, and a spectroscopic reference state for estimating the stability of related peptides in solution.