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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Peptide folding and aggregation studied using a simplified atomic model

Author

  • Anders Irbäck

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

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