Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach

• DOI: 10.1126/science.8502992
• Publication Date: 2006-10-05T23:05:09Z
• Authors: Angel C. de Dios; John G. Pearson; Eric Oldfield
• Keywords: Electrostatics; Chemical shift

Recent theoretical developments permit the prediction of 1H, 13C, 15N, and 19F nuclear magnetic resonance chemical shifts in proteins offer new ways analyzing secondary tertiary structure as well for probing protein electrostatics. For phi, psi torsion angles dominate shielding C alpha beta, but addition hydrogen bonding electrostatics gives even better accord with experiment. 15NH, side chain (chi 1) are also important, nearest neighbor sequence effects, whereas 1HN, is particularly significant. 19F, weak or long-range electrostatic fields nonequivalencies. The ability to predict from known test structures opens avenues refinement determination, especially condensed systems.