2001/01/01 by Olivier Collet, O Collet · 3 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · Physics and Astronomy · #Crystallography and molecular interactions #Enzyme Structure and Function #Protein Structure and Dynamics #cond-mat.soft #q-bio
paper · pdf · doi:10.1209/epl/i2001-00128-3
published as Europhys. Lett. 53 (1), pp 93-99 (2001) · 7 pages, 2 figures
openalex publication_date 2001/01/01 · arxiv created 2001/01/17 · arxiv updated 2009/11/30 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/04
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 p H 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.