Volume 53, Number 1, January 2001
|Page(s)||93 - 99|
|Section||Interdisciplinary physics and related areas of science and technology|
|Published online||01 December 2003|
Warm and cold denaturation in the phase diagram of a protein lattice model
Laboratoire de Chimie Théorique, UMR CNRS 7565,
Faculté des Sciences
Université Henri Poincaré-Nancy 1 -
54506 Vandoeuvre-lès-Nancy, France
Accepted: 20 October 2000
Studying the properties of the solvent around proteins, we propose a much more sophisticated model of solvation than temperature-independent pairwise interactions between monomers, as is used commonly in lattice representations. We applied our model of solvation to a 16-monomer chain constrained on a two-dimensional lattice. We compute a phase diagram function of the temperature and a solvent parameter which is related to the pH of the solution. It exhibits a native state in which the chain coalesces into a unique compact conformation as well as a denatured state. Under certain solvation conditions, both warm and cold denaturations occur between the native and the denatured states. A good agreement is found with the data obtained from calorimetric experiments, thereby validating the proposed model.
PACS: 87.10.+e – General theory and mathematical aspects / 87.14.Ee – Proteins / 64.60.Cn – Order-disorder transformations; statistical mechanics of model systems
© EDP Sciences, 2001
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