Improved Peptide and Protein Torsional Energetics with the OPLS-AA Force Field

By M. Robertson, Julian Tirado-Rives, W. L. Jorgensen. Journal of Chemical Theory and Computation, 2015

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The development and validation of new peptide dihedral parameters are reported for the OPLS-AA force field. High accuracy quantum chemical methods were used to scan φ, ψ, χ1, and χ2 potential energy surfaces for blocked dipeptides. New Fourier coefficients for the dihedral angle terms of the OPLS-AA force field were fit to these surfaces, utilizing a Boltzmann-weighted error function and systematically examining the effects of weighting temperature. To prevent overfitting to the available data, a minimal number of new residue-specific and peptide-specific torsion terms were developed. Extensive experimental solution-phase and quantum chemical gas-phase benchmarks were used to assess the quality of the new parameters, named OPLS-AA/M, demonstrating significant improvement over previous OPLS-AA force fields. A Boltzmann weighting temperature of 2000 K was determined to be optimal for fitting the new Fourier coefficients for dihedral angle parameters. Conclusions are drawn from the results for best practices for developing new torsion parameters for protein force fields.

Subfields: Atomic and Molecular Physics, and Optics, Electrical and Electronic Engineering, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1a232ada436f72932456409d542f6f727b7e3ba0

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In Atomic and Molecular Physics, and Optics

  1. Leela S. Dodda
  2. Julian Tirado-Rives
  3. W. L. Jorgensen

In Molecular Biology

  1. Leela S. Dodda
  2. Israel Cabeza de Vaca
  3. W. L. Jorgensen
  4. Julian Tirado-Rives
  5. Zoe Cournia

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