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Minimum model for the α‐helix–β‐hairpin transition in proteins
Author(s) -
Imamura Hideo,
Chen Jeff Z. Y.
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21216
Subject(s) - transition (genetics) , helix (gastropod) , biophysics , chemistry , crystallography , biology , biochemistry , ecology , gene , snail
We present a minimal model for proteins, which is able to capture the structural conversion between the α‐helix and β‐hairpin. In most regimes of the parameter space, the model produces a stable structure at a low temperature; in a few limited regimes of the parameter space, the model displays an β‐hairpin transition as the physical conditions vary. These variations include a perturbation on hydrogen bonding propensity at the middle of the modeled chain, or the change of the hydrophobicity of a designated pair along the chain. Using Monte Carlo simulations, we demonstrate the structural conversion by means of state diagrams, heat capacity maps, and free energy maps. Proteins 2007. © 2007 Wiley‐Liss, Inc.