
Anders Irbäck
Professor

Folding thermodynamics of peptides
Author
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 - Undergoing reorganization
- Department of Astronomy and Theoretical Physics - Undergoing reorganization
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