Conformational conversion of proteins due to mutation

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2004 EDP Sciences
, , Citation H. Imamura and J. Z. Y. Chen 2004 EPL 67 491 DOI 10.1209/epl/i2003-10289-5

0295-5075/67/3/491

Abstract

We present a potential-energy model that successfully reproduces the hydrogen bonding effect in proteins and can be used to represent well-defined secondary structures, both α-helices and β-sheets. We discuss the mechanism of conformational conversion, specifically between an α-helix and a β-hairpin, caused by sequence perturbation in monomer type. The thermodynamics and kinetics of the model were analyzed by the Monte Carlo simulation technique.

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10.1209/epl/i2003-10289-5