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Many commonly used force fields for protein systems such as AMBER, CHARMM,GROMACS, OPLS, and ECEPP have amino-acid-independent force-field parameters ofmain-chain torsion-energy terms. Here, we propose a new type ofamino-acid-dependent torsion-energy terms in the force fields. As an example,we applied this approach to AMBER ff03 force field and determined newamino-acid-dependent parameters for $\psi$ and $\psi'$ angles for each aminoacid by using our optimization method, which is one of the knowledge-basedapproach. In order to test the validity of the new force-field parameters, wethen performed folding simulations of $\alpha$-helical and $\beta$-hairpinpeptides, using the optimized force field. The results showed that the newforce-field parameters gave structures more consistent with the experimentalimplications than the original AMBER ff03 force field.

Amino-acid-dependent main-chain torsion-energy terms for protein systems