Publication | Open Access
Are Free Energy Calculations Useful in Practice? A Comparison with Rapid Scoring Functions for the p38 MAP Kinase Protein System
223
Citations
14
References
2001
Year
A ComparisonEngineeringMolecular BiologyComputational ChemistryMolecular DesignProtein FoldingReceptor Tyrosine KinaseProteomicsBiochemistryPrediction MethodProtein ModelingFree Energy SimulationsProtein BioinformaticsProtein PhosphorylationRapid Scoring FunctionsNatural SciencesMolecular PropertyComputational BiologyRational Drug DesignRelative Free EnergyCellular BiochemistrySystems BiologyMolecular DockingDrug DiscoveryComputational Biophysics
Precise thermodynamic integration free energy simulations have been applied to a congeneric series of 16 inhibitors to the p38 MAP kinase protein for which the experimental binding data (IC(50)) is known. The relative free energy of binding for each compound has been determined. For comparison, the same series of compounds have also scored using the best rapid scoring functions used in database screening. From the results of these calculations, we find (1) that precise free energy simulations allow predictions that are reliable and in good agreement with experiment; (2) that predictions of lower reliability, but still in good qualitative agreement with experiment, can be obtained using the OWFEG free energy grid method, at a much lower computational cost; (3) and that other methods, not based on free energy simulations yield results in much poorer agreement with experiment. A new predictive index, which measures the reliability of a prediction method in the context of normal use, is defined and calculated for each scoring method. Predictive indices of 0.84, 0.56, 0.04, -0.05, and 0.25 are calculated for thermodynamic integration, OWFEG, ChemScore, PLPScore, and Dock Energy Score, respectively, where +1.0 is perfect correct prediction, -1.0 is perfect incorrect prediction, and 0.0 is random.
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