1H-NMR studies on nucleotide binding to the sarcoplasmic reticulum Ca2+ ATPase. Determination of the conformations of bound nucleotides by the measurement of proton-proton transferred nuclear Overhauser enhancements.

@article{Clore19821HNMRSO,
  title={1H-NMR studies on nucleotide binding to the sarcoplasmic reticulum Ca2+ ATPase. Determination of the conformations of bound nucleotides by the measurement of proton-proton transferred nuclear Overhauser enhancements.},
  author={G Marius Clore and Angela M. Gronenborn and C Mitchinson and N. Michael Green},
  journal={European journal of biochemistry},
  year={1982},
  volume={128 1},
  pages={113-17}
}
The glycosidic bond torsion angles and the conformations of the ribose of Mg2+ATP, Mg2+ADP and Mg2+AdoPP[NH]P (magnesium adenosine 5'-[beta, gamma-imido]triphosphate) bound to Ca2+ATPase, both native and modified with fluorescein isothiocyanate (FITC), in intact sarcoplasmic reticulum have been determined by the measurement of proton-proton transferred nuclear Overhauser enhancements by 1H-NMR spectroscopy. This method shows clearly the existence of a low-affinity ATP binding site after… CONTINUE READING

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Cold Spring Harbor Quant

C. R. Jones, C. T. Sikakana, S. Hehir, M.-C. Kuo, W. A. Gibbons
Biol • 1971

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