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Hydrogen bonding effects on 31 P NMR shielding in the pyrophosphate group of NADPH bound to L. casei dihydrofolate reductase
Author(s) -
Gerothanassis I.P.,
Birdsall B.,
Feeney J.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81094-o
Subject(s) - chemistry , dihydrofolate reductase , pyrophosphate , hydrogen bond , stereochemistry , proton nmr , crystallography , electromagnetic shielding , enzyme , molecule , biochemistry , physics , organic chemistry , quantum mechanics
A comparison of 31 P 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 31 P shielding of the pyrophosphate nuclei whereas changes in P‐O‐C 5 ‐H 5 ' torsion angle have little effect.