Helix formation and folding in an artificial peptide

We study the relation between α-helix formation and folding for a simple artificial peptide, Ala10–Gly5–Ala10. Our data rely on multicanonical Monte Carlo simulations where the interactions among all atoms are taken into account. The free-energy landscape of the peptide is evaluated for various temp...

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Bibliographic Details
Published in:The Journal of chemical physics 2002-08, Vol.117 (5), p.2337-2343
Main Authors: Alves, Nelson A., Hansmann, Ulrich H. E.
Format: Article
Language:English
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Summary:We study the relation between α-helix formation and folding for a simple artificial peptide, Ala10–Gly5–Ala10. Our data rely on multicanonical Monte Carlo simulations where the interactions among all atoms are taken into account. The free-energy landscape of the peptide is evaluated for various temperatures. Our data indicate that folding of this peptide is a two-step process. In the first step two α-helices are formed which afterwards re-arrange themselves into a U-like structure.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.1489419