Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation.

@article{Best2012InclusionOM,
  title={Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation.},
  author={Robert B. Best and Jeetain Mittal and Michael Feig and Alexander D. MacKerell},
  journal={Biophysical journal},
  year={2012},
  volume={103 5},
  pages={1045-51}
}
Folding simulations on peptides and proteins using empirical force fields have demonstrated the sensitivity of the results to details of the backbone potential. A recently revised version of the additive CHARMM protein force field, which includes optimization of the backbone CMAP potential to achieve good balance between different types of secondary structure, correcting the α-helical bias present in the former CHARMM22/CMAP energy function, is shown to result in improved cooperativity for the… CONTINUE READING

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