NMR-Based Protein Potentials

摘要

The quality of molecular mechanics force fields is vital for the accurate in silico characterization of proteins. However, the development of better force fields has been a formidable challenge. Important improvements in force fields have been made recently; for example, CHARMM22/CMAP and Amber's ff99SB have been validated for several proteins by comparison of experimental NMR data, including spin relaxation data and dipolar couplings. with those predicted by molecular dynamics (MD) simulations. Another type of NMR observable is the chemical shift whose relationship to three-dimensional (3D) protein structures is increasingly well understood. A recent comparison of calculated and experimental protein ~(13)C chemical shifts suggests that there is considerable room for additional improvements of the force field.