@article{oai:nagoya.repo.nii.ac.jp:00026925,
 author = {Sakae, Yoshitake and Okamoto, Yuko},
 issue = {6},
 journal = {The Journal of Chemical Physics},
 month = {Feb},
 note = {Many commonly used force fields for protein systems such as AMBER, CHARMM, GROMACS, OPLS, and ECEPP have amino-acid-independent force-field parameters for main-chain torsion-energy terms. Here, we propose a new type of amino-acid-dependent torsion-energy terms in the force fields. As an example, we applied this approach to AMBER ff03 force field and determined new amino-acid-dependent parameters for ψ (N-C^α-C-N) and ζ (C^β-C^α-C-N) angles for each amino acid by using our optimization method, which is one of the knowledge-based approach. In order to test the validity of the new force-field parameters, we then performed folding simulations of α-helical and β-hairpin peptides, using the optimized force field. The results showed that the new force-field parameters gave structures more consistent with the experimental implications than the original AMBER ff03 force field.},
 title = {Amino-acid-dependent main-chain torsion-energy terms for protein systems},
 volume = {138},
 year = {2013}
}