| Issue |
Europhys. Lett.
Volume 39, Number 5, September I 1997
|
|
|---|---|---|
| Page(s) | 575 - 580 | |
| Section | Cross-disciplinary physics and related areas of science and technology | |
| DOI | https://doi.org/10.1209/epl/i1997-00397-8 | |
| Published online | 01 September 2002 | |
Hydration effects in a lattice model of protein folding
Laboratoire de Biophysique Moleculaire, Université H. Poincaré Nancy 1,
Faculté des Sciences, BP 239-54506, Vandoeuvre-lès-Nancy, France
Received:
14
January
1997
Accepted:
16
July
1997
The problem of protein folding is approached by introducing explicit solvent effects on a lattice model of chains composed of hydrophobic and polar units. The free energy and entropy of the chain hydration are defined using different values for the contact energy between units. Results obtained from an exhaustive exploration, on a 2D lattice, of the complete set of conformations and possible sequences of 10 unit chains, show that hydration decreases the degeneracy of the ground state of certain sequences, thus allowing a better selection between the specific sequences which present a low free energy and compact structures.
PACS: 87.10.+e – General, theoretical, and mathematical biophysics (including logic of biosystems, quantum biology, and relevant aspects of thermodynamics, information theory, cybernetics, and bionics) / 87.15.By – Structure, bonding, conformation, configuration, and isomerism of bi omo le cu les
© EDP Sciences, 1997
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