Jing Huang and Alexander D. MacKerell Jr
Protein structure and dynamics can be characterized on the atomistic level with both NMR experiments and molecular dynamics (MD) simulations. The ability of the CHARMM36 (C36) force field (FF) to reproduce various NMR observables using MD simulations is quantified. The studied NMR properties include backbone scalar couplings across hydrogen bonds, residual dipolar couplings (RDCs), and relaxation order parameters, as well as scalar couplings, RDCs, and order parameters for side-chain amino- and methyl-containing groups. The C36 FF leads to better correlation with experimental data compared to the CHARMM22/CMAP FF, suggesting the use of C36 in protein simulations.