Helix Formation and Folding in an Artificial Peptide

Details Helix Formation and Folding in an Artificial Peptide Helix Formation and Folding in an Artificial Peptide

2002-05-27

arxiv.org/abs/cond-mat/0205559v1

Physics

Condensed Matter

Statistical Mechanics

15 pages, with 9 eps figures

Scientific paper

10.1063/1.1489419

We study the relation between $\alpha$-helix formation and folding for a simple artificial peptide, Ala$_{10}$-Gly$_5$-Ala$_{10}$. 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 a first step two $\alpha$-helices are formed which afterwards re-arrange themselves into a U-like structure.

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