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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Folding thermodynamics of peptides

Author

  • Anders Irbäck
  • Sandipan Mohanty

Summary, in English

A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with; 20 residues each. The test set contains both alpha-helical ( Trp cage, F-s) and beta-sheet ( GB1p, GB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely sequence-based, is able to fold these different peptides for one and the same choice of model parameters. Furthermore, the melting behavior of the peptides is in good quantitative agreement with experimental data. Apparent folded populations obtained using different observables are compared, and are found to be very different for some of the peptides ( e. g., Betanova). In other cases ( in particular, GB1m2 and GB1m3), the different estimates agree reasonably well, indicating a more two-state-like melting behavior.

Department/s

  • Computational Biology and Biological Physics
  • Department of Astronomy and Theoretical Physics

Publishing year

2005

Language

English

Pages

1560-1569

Publication/Series

Biophysical Journal

Volume

88

Issue

3

Document type

Journal article

Publisher

Cell Press

Topic

  • Biophysics

Status

Published

ISBN/ISSN/Other

  • ISSN: 1542-0086