Folding thermodynamics of three beta-sheet peptides: A model study

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dc.creatorIrbäck, Anders
dc.creatorSjunnesson, Fredrik
dc.date2003-12-30
dc.date.accessioned2026-07-07T05:58:05Z
dc.date.available2026-07-07T05:58:05Z
dc.descriptionWe 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.
dc.description17 pages, 7 figures, to appear in Proteins
dc.identifierhttps://arxiv.org/abs/q-bio/0312042
dc.identifierhttp://arxiv.org/abs/q-bio/0312042
dc.identifierProteins 56 (2004) 110-116
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88230
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.titleFolding thermodynamics of three beta-sheet peptides: A model study
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