The Journal of Physical Chemistry B · 1999 · 375 citations · 23 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryComputational BiophysicsComputational ChemistryComputational Molecular BiophysicsElectrostatics In BiomoleculesForce FieldsMolecular DynamicsMolecular ModelingProtein StructureBorn Solvation ModelElectrostatic SolvationElectrostatic Solvation Free EnergyGeneralized Born ModelsMolecular Dynamics Simulations Of Nucleic AcidsNucleic Acid SimulationsSolvation Free EnergySolvation In Biomolecular Simulations
The generalized Born model proposed by Still and co-workers (Qui, D.; Shenkin, P. S.; Hollinger, F. P.; Still, W. C. J. Phys. Chem. A 1997, 101, 3005−3014) is parametrized specifically for proteins, peptides, and nucleic acids within the CHARMM all hydrogen and polar hydrogen force fields. A database of atomic electrostatic environments and molecular electrostatic solvation free energies comprising amino acid residues, nucleic acid bases, dipeptides, dinucleotides, proteins, and DNA strands is established, and numerical finite difference Poisson calculations are solved using atomic radii and charges from the corresponding force field parameters. These data provide the necessary input to parametrize generalized Born models for a particular force field. The performance of these models in reproducing overall molecular solvation trends is examined and found to be quite good. Furthermore, calculations of electrostatic solvation free energy differences suggest that conformational free energy changes are well reproduced. Finally, the utilization of this generalized Born model in molecular dynamics simulations (both with and without cutoffs) is shown to give excellent agreement with explicit solvent simulations of a small 56-residue protein in water.
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Optimization by Simulated Annealing
Scott Kirkpatrick, C. D. Gelatt, M.P. Vecchi · Science · 1983 · 44.6K citations