Helix Formation and Folding in an Artificial Peptide
arXiv:cond-mat/0205559 · doi:10.1063/1.1489419
Abstract
We study the relation between $α$-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 $α$-helices are formed which afterwards re-arrange themselves into a U-like structure.
15 pages, with 9 eps figures