Solvation model dependency of helix-coil transition in polyalanine

Abstract

Helix-coil transitions in poly-alanine molecules of length 10 are studied by multicanonical Monte Carlo simulations. The solvation effects are included by either a distance-dependent dielectric permittivity or by a term that is proportional to the solvent-accessible surface area of the peptide. We found a strong dependence of the characteristics of the helix-coil transition from the details of the solvation model.

to appear in Biophysical Journal

References in corpus (1)

• Yang-Lee zeros and the helix-coil transition in a continuum model of polyalanine

Cited by in corpus (6)

• Solution effects and the order of the helix-coil transition in polyalanine
• Helix Formation and Folding in an Artificial Peptide
• Helix vs. Sheet Formation in a Small Peptide
• On the Helix-coil Transition in Alanine-based Polypeptides in Gas Phase
• Metropolis simulations of Met-Enkephalin with solvent-accessible area parameterizations
• Rugged Metropolis Sampling with Simultaneous Updating of Two Dynamical Variables