Peptide folding and aggregation studied using a simplified atomic model
Författare
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.
Publiceringsår
2005
Språk
Engelska
Sidor
1553-1564
Publikation/Tidskrift/Serie
Journal of Physics: Condensed Matter
Volym
17
Issue
18
Dokumenttyp
Artikel i tidskrift
Förlag
IOP Publishing
Ämne
- Biophysics
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1361-648X