2004/11/12 by Buddhapriya Chakrabarti, Buddhapriya Chakrabartiand, Chakrabarti, Buddhapriya +2
Biochemistry, Genetics and Molecular Biology · Engineering · Materials Science · Physics and Astronomy · #FOS: Physical sciences #Gear and Bearing Dynamics Analysis #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft) #Statistical Mechanics (cond-mat.stat-mech) #Supramolecular Self-Assembly in Materials #cond-mat.soft #cond-mat.stat-mech
paper · pdf · doi:10.48550/arxiv.cond-mat/0411358
10 pages, 7 eps figures
arxiv created 2004/11/12 · openalex publication_date 2004/11/12 · arxiv updated 2009/12/01 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28
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.