Improved treatment of the protein backbone in empirical force fields.

摘要: Empirical force field-based calculations of proteins, including protein-folding studies, have improved our understanding the relationship their structure to biological function. However, limitations in accuracy empirical fields treatment peptide backbone exist. Presented is a grid correction approach improve φ/ψ conformational energies. Inclusion this with CHARMM22 all-atom protein field shown lead significant improvement energies both model compound, alanine dipeptide, and proteins crystal environment. The developed suggested improvements treat peptides proteins.