We revisit the parameterization of the intramolecular part of the AMBER protein force field by using data from systematic scanning of the potential energy surface of amino acid dipeptides and the ForceBalance parameterization software. We found that AMBER force field accurately estimates potential energies near the minima, but systematically overestimates energies in the higher energy regions. The new intramolecular parameter set, dubbed AMBER15-FB, is validated using simulations of equilibrium structures, NMR order parameters, protein melting, protein folding, and the denatured state ensemble. We recommend the combination of the AMBER15-FB and TIP3P-FB water models for general purpose simulations of protein dynamics.

Systematic improvement of intramolecular parameters for protein force fields from quantum chemistry data

251st National Meeting (2016)

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