Helix Formation and Folding in an Artificial Peptide

Abstract

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.

15 pages, with 9 eps figures

References in corpus (4)

• Solvation model dependency of helix-coil transition in polyalanine
• Yang-Lee zeros and the helix-coil transition in a continuum model of polyalanine
• Numerical comparison of two approaches for the study of phase transitions in small systems
• Thermodynamics and Kinetics of Folding of a Small Peptide

Cited by in corpus (3)

• Multicanonical Study of Coarse-Grained Off-Lattice Models for Folding Heteropolymers
• Helix vs. Sheet Formation in a Small Peptide
• Generalized-Ensemble Simulations of the Human Parathyroid Hormone Fragment PTH(1-34)