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

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

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