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Empirical Force Field (empirical + force_field)
Selected AbstractsComparison of implicit solvent models for the simulation of protein,surface interactionsJOURNAL OF COMPUTATIONAL CHEMISTRY, Issue 16 2006Yu Sun Abstract Empirical force field-based molecular simulations can provide valuable atomistic-level insights into protein,surface interactions in aqueous solution. While the implicit treatment of solvation effects is desired as a means of improving simulation efficiency, existing implicit solvent models were primarily developed for the simulation of peptide or protein behavior in solution alone, and thus may not be appropriate for protein interactions with synthetic material surfaces. The objective of this research was to calculate the change in free energy as a function of surface,separation distance for peptide,surface interactions using different empirical force field-based implicit solvation models (ACE, ASP, EEF1, and RDIE with the CHARMM 19 force field), and to compare these results with the same calculations conducted using density functional theory (DFT) combined with the self-consistent reaction field (SCRF) implicit solvation model. These comparisons show that distinctly different types of behavior are predicted with each implicit solvation method, with ACE providing the best overall agreement with DFT/SCRF calculations. These results also identify areas where ACE is in need of improvement for this application and provide a basis for subsequent parameter refinement. © 2006 Wiley Periodicals, Inc. J Comput Chem, 2006 [source] Peptide T exhibits a well-defined structure in fluorinated solvent at low temperatureJOURNAL OF PEPTIDE SCIENCE, Issue 12 2009Tran-Chin Yang Abstract The structure of Peptide T was determined by solution NMR spectroscopy, under strong structure-inducing conditions: 40% hexafluoro-2-propanol aqueous solution at 5 °C. Under these conditions it was possible to detect medium-range NOEs for the first time for this peptide. This allowed a much better-defined structure to be determined for Peptide T in comparison with earlier NMR and computational studies. Peptide structures consistent with the experimental restraints were generated using a restrained MD simulation with a full empirical force field. Residues 4,8 of Peptide T take on a well-defined structure with a heavy atom RMSD of 0.78 Å. The structure is stabilized by hydrogen bonding to side-chain oxygen atoms of Thr 4 and Thr 8, as well as backbone hydrogen bonding between residues 5 and 7 that forms this region into a classic ,-turn. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd. [source] A computationally inexpensive modification of the point dipole electrostatic polarization model for molecular simulationsJOURNAL OF COMPUTATIONAL CHEMISTRY, Issue 3 2003George A. Kaminski Abstract We present an approximation, which allows reduction of computational resources needed to explicitly incorporate electrostatic polarization into molecular simulations utilizing empirical force fields. The proposed method is employed to compute three-body energies of molecular complexes with dipolar electrostatic probes, gas-phase dimerization energies, and pure liquid properties for five systems that are important in biophysical and organic simulations,water, methanol, methylamine, methanethiol, and acetamide. In all the cases, the three-body energies agreed with high level ab initio data within 0.07 kcal/mol, dimerization energies,within 0.43 kcal/mol (except for the special case of the CH3SH), and computed heats of vaporization and densities differed from the experimental results by less than 2%. Moreover, because the presented method allows a significant reduction in computational cost, we were able to carry out the liquid-state calculations with Monte Carlo technique. Comparison with the full-scale point dipole method showed that the computational time was reduced by 3.5 to more than 20 times, depending on the system in hand and on the desired level of the full-scale model accuracy, while the difference in energetic results between the full-scale and the presented approximate model was not great in the most cases. Comparison with the nonpolarizable OPLS-AA force field for all the substances involved and with the polarizable POL3 and q90 models for water and methanol, respectively, demonstrates that the presented technique allows reduction of computational cost with no sacrifice of accuracy. We hope that the proposed method will be of benefit to research employing molecular modeling technique in the biophysical and physical organic chemistry areas. © 2003 Wiley Periodicals, Inc. J Comput Chem 24: 267,276, 2003 [source] | ||||||||||