The nonlinear elasticity of an $α$-helical polypeptide: Monte Carlo studies

Details The nonlinear elasticity of an $α$-helical polypeptide: Monte Carlo studies The nonlinear elasticity of an $α$-helical polypeptide: Monte Carlo studies

2004-11-12

arxiv.org/abs/cond-mat/0411358v1

Physics

Condensed Matter

Soft Condensed Matter

10 pages, 7 eps figures

Scientific paper

We perform Monte Carlo simulations to study the elastic properties of the helix-coil worm-like chain model of alpha-helical polypeptides. In this model the secondary structure enters as a scalar (Ising like) variable that controls the local chain bending modulus. We compute numerically the bending and stretching compliances of this molecule as well as the nonlinear interaction between stretching and torque over a wide range of model parameters. The numerical results agree well with previous mean-field and perturbative calculations where they are expected to do so. The Monte Carlo simulations allow us to examine the response of the chain to large forces and torques where the perturbative approaches fail. In addition we extend our mean-field analysis by studying the fluctuation dominated regime at the force-induced denaturation transition.

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