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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

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

Author

  • Anders Irbäck
  • Fredrik Sjunnesson

Summary, in English

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. (C) 2004 Wiley-Liss, Inc.

Department/s

  • Computational Biology and Biological Physics

Publishing year

2004

Language

English

Pages

110-116

Publication/Series

Proteins

Volume

56

Issue

1

Document type

Journal article

Publisher

John Wiley and Sons

Topic

  • Biophysics

Keywords

  • Monte Carlo simulation
  • beta-hairpin
  • protein folding
  • three-stranded beta-sheet
  • all-atom
  • model

Status

Published

ISBN/ISSN/Other

  • ISSN: 0887-3585