| Issue |
Europhys. Lett.
Volume 67, Number 3, August 2004
|
|
|---|---|---|
| Page(s) | 491 - 497 | |
| Section | Interdisciplinary physics and related areas of science and technology | |
| DOI | https://doi.org/10.1209/epl/i2003-10289-5 | |
| Published online | 01 July 2004 | |
Conformational conversion of proteins due to mutation
Department of Physics, University of Waterloo Waterloo, Ontario, Canada N2L 3G1
Received:
27
November
2003
Accepted:
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 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.
PACS: 87.15.He – Dynamics and conformational changes / 87.15.Aa – Theory and modeling; computer simulation / 87.15.By – Structure and bonding
© EDP Sciences, 2004
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