Anders Irbäck and Fredrik Sjunnesson
Folding Thermodynamics of Three Beta-Sheet
Peptides: A Model Study
Proteins: Structure, Function, and Bioinformatics
56, 110-116 (2004)
Abstract
We study the folding thermodynamics of a beta-hairpin and
two three-stranded beta-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 beta-hairpin.
LU TP 03-40
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