The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin.

@article{Jorgensen1988TheO,
  title={The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin.},
  author={W. L. Jorgensen and J. Tirado-Rives},
  journal={Journal of the American Chemical Society},
  year={1988},
  volume={110 6},
  pages={
          1657-66
        }
}
A complete set of intermolecular potential functions has been developed for use in computer simulations of proteins in their native environment. Parameters are reported for 25 peptide residues as well as the common neutral and charged terminal groups. The potential functions have the simple Coulomb plus Lennard-Jones form and are compatible with the widely used models for water, TIP4P, TIP3P, and SPC. The parameters were obtained and tested primarily in conjunction with Monte Carlo statistical… Expand
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References

SHOWING 1-10 OF 54 REFERENCES
Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin.
  • M. Teeter
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1984
An all atom force field for simulations of proteins and nucleic acids
...
1
2
3
4
5
...