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

FEBS Letters

Birdsall, B.¹  Feeney, J.¹  Gerothanassis, I.P.¹ 

[1] Laboratory of Molecular Structure, National Institute of Medical Research, Mill Hill, London NW7 1AA, UK

关键词: 31P NMR;    NADPH;    DHFR;    Solvation;   

DOI  :  10.1016/0014-5793(91)81094-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown