Hydrogen bonding effects on 31P NMR shielding in the pyrophosphate group of NADPH bound to L. casei dihydrofolate reductase

Abstract
A comparison of 31P NMR chemical shift data and X‐ray structural data [Filman, D.J., Bolin, J.T., Matthews, D.A. and Kraut, J. (1982) J. Biol. Chem. 257, 13663–13672] for complexes of NADPH with L. casei dihydrofolate reductase indicates that solvation effects play a major role in influencing the 31P shielding of the pyrophosphate nuclei whereas changes in P‐O‐C5‐H5' torsion angle have little effect.

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