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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.
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Alves et al. (2002) studied this question.
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