A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6

Oostenbrink, C., Villa, A., Mark, A. E. and Van Gunsteren, W. F. (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. Journal of Computational Chemistry, 25 13: 1656-1676.


Author Oostenbrink, C.
Villa, A.
Mark, A. E.
Van Gunsteren, W. F.
Title A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
Journal name Journal of Computational Chemistry   Check publisher's open access policy
ISSN 0192-8651
Publication date 2004-10
Year available 2004
Sub-type Article (original research)
DOI 10.1002/jcc.20090
Volume 25
Issue 13
Start page 1656
End page 1676
Total pages 21
Place of publication Hoboken
Publisher John Wiley & Sons Inc
Language eng
Abstract Successive parameterizations of the GROMOS force field have been used successfully to simulate biomolecular systems over a long period of time. The continuing expansion of computational power with time makes it possible to compute ever more properties for an increasing variety of molecular systems with greater precision. This has led to recurrent parameterizations of the GROMOS force field all aimed at achieving better agreement with experimental data. Here we report the results of the latest, extensive reparameterization of the GROMOS force field. In contrast to the parameterization of other biomolecular force fields, this parameterization of the GROMOS force field is based primarily on reproducing the free enthalpies of hydration and apolar solvation for a range of compounds. This approach was chosen because the relative free enthalpy of solvation between polar and apolar environments is a key property in many biomolecular processes of interest, such as protein folding, biomolecular association, membrane formation, and transport over membranes. The newest parameter sets, 53A5 and 53A6, were optimized by first fitting to reproduce the thermodynamic properties of pure liquids of a range of small polar molecules and the solvation free enthalpies of amino acid analogs in cyclohexane (53A5). The partial charges were then adjusted to reproduce the hydration free enthalpies in water (53A6). Both parameter sets are fully documented, and the differences between these and previous parameter sets are discussed. (C) 2004 Wiley Periodicals, Inc.
Keyword Chemistry, Multidisciplinary
GROMOS force field
force-field parameterization
free-energy calculation
solvation
hydration
Molecular-dynamics Simulations
Free-energy Calculations
Human Alpha-lactalbumin
Side-chain Analogs
Computer-simulation
Nucleic-acids
N-alkanes
Thermodynamic Properties
Conformational Dynamics
Dimethyl-sulfoxide
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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