Exploring peptide energy landscapes: a test of force fields and implicit solvent models.

@article{Steinbach2004ExploringPE,
  title={Exploring peptide energy landscapes: a test of force fields and implicit solvent models.},
  author={Peter J. Steinbach},
  journal={Proteins},
  year={2004},
  volume={57 4},
  pages={665-77}
}
A biased Monte Carlo-minimization/annealing conformational search was used to characterize five descriptions of the energy landscape for each of three model systems: the 20-residue "trp-cage" miniprotein, the 20-residue "BS1" peptide, and the 17-residue "U(1-17)T9D" peptide. The EEF1 and SASA energy landscapes were studied as well as those defined by using the GB/ACE implicit water model with one of three protein force fields: CHARMM19, CHARMM22, and CHARMM22/CMAP. The lowest-energy structures… CONTINUE READING