Anders Irbäck
Peptide Folding and Aggregation Studied Using a Simplifed Atomic Model
Journal of Physics: Condensed Matter 17, S1553-S1564 (2005)

Abstract
Using an atomic model with a simplified sequence-based potential, the folding properties of several different peptides are studied. Both α-helical (Trp cage, Fs) and β-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 Aβ peptide is studied, with very promising results.

LU TP 04-31