Europhys. Lett.
Volume 67, Number 3, August 2004
Page(s) 491 - 497
Section Interdisciplinary physics and related areas of science and technology
Published online 01 July 2004
Europhys. Lett., 67 (3), pp. 491-497 (2004)
DOI: 10.1209/epl/i2003-10289-5

Conformational conversion of proteins due to mutation

H. Imamura and J. Z. Y. Chen

Department of Physics, University of Waterloo Waterloo, Ontario, Canada N2L 3G1

(Received 27 November 2003; accepted in final form 12 May 2004)

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 $\alpha$-helices and $\beta$-sheets. We discuss the mechanism of conformational conversion, specifically between an $\alpha$-helix and a $\beta$-hairpin, caused by sequence perturbation in monomer type. The thermodynamics and kinetics of the model were analyzed by the Monte Carlo simulation technique.

87.15.He - Dynamics and conformational changes.
87.15.Aa - Theory and modeling; computer simulation.
87.15.By - Structure and bonding.

© EDP Sciences 2004