
Anders Irbäck
Professor

Peptide folding and aggregation studied using a simplified atomic model
Author
Summary, in English
Using an atomic model with a simplified-sequence-based potential, the folding properties of several different peptides are studied. Both alpha-helical (Trp cage, F-s) and beta-sheet(GB1p, GB1m2, GB1m3, Betanova, LLM) peptides are considered. The model is able to fold these different peptides for one and the same choice of;parameters, and the melting behaviour of the peptides (folded population against temperature) is in very good agreement with experimental data. Furthermore, using the same model with unchanged parameters, the aggregation behaviour of a fibril-forming fragment of the Alzheimer's A beta peptide is studied, with very promising results.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
Publishing year
2005
Language
English
Pages
1553-1564
Publication/Series
Journal of Physics: Condensed Matter
Volume
17
Issue
18
Document type
Journal article
Publisher
IOP Publishing
Topic
- Biophysics
Status
Published
ISBN/ISSN/Other
- ISSN: 1361-648X