Peptide folding and aggregation studied using a simplified atomic model

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Abstract

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.
Original languageEnglish
Pages (from-to)S1553-S1564
JournalJournal of Physics: Condensed Matter
Volume17
Issue number18
DOIs
Publication statusPublished - 2005

Subject classification (UKÄ)

  • Biophysics

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