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Folding thermodynamics of three β‐sheet peptides: A model study
Author(s) -
Irbäck Anders,
Sjunnesson Fredrik
Publication year - 2004
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.20157
Subject(s) - thermodynamics , folding (dsp implementation) , chemistry , physics , engineering , mechanical engineering
We study the folding thermodynamics of a β‐hairpin and two three‐stranded β‐sheet peptides using a simplified sequence‐based all‐atom model, in which folding is driven mainly by backbone hydrogen bonding and effective hydrophobic attraction. The native populations obtained for these three sequences are in good agreement with experimental data. We also show that the apparent native population depends on which observable is studied; the hydrophobicity energy and the number of native hydrogen bonds give different results. The magnitude of this dependence matches well with the results obtained in two different experiments on the β‐hairpin. Proteins 2004. © 2004 Wiley‐Liss, Inc.