31P-NMR spectra of the Ha-ras p21.nucleotide complexes

Rösch, Paul; Wittinghofer, Alfred; Tucker, J.; Sczakiel, Georg; Lebermann, Reuben; Schlichting, Ilme

doi:10.1016/0006-291X(86)90029-X

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31P-NMR spectra of the Ha-ras p21.nucleotide complexes

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Rösch, Paul
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer, Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Sczakiel, Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting, Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0006291X8690029X/pdf?md5=21264002c83a587eb5734011b3cbdfce&pid=1-s2.0-0006291X8690029X-main.pdf
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https://doi.org/10.1016/0006-291X(86)90029-X
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引用

Rösch, P., Wittinghofer, A., Tucker, J., Sczakiel, G., Lebermann, R., & Schlichting, I. (1986). 31P-NMR spectra of the Ha-ras p21.nucleotide complexes. Biochemical and Biophysical Research Communications, 135(2), 549-555. doi:10.1016/0006-291X(86)90029-X.

引用: https://hdl.handle.net/11858/00-001M-0000-0019-AEC8-D

要旨

Phosphorus nuclear magnetic resonance spectra of the Ha-ras oncogene product p21 and its nucleotide complexes have been obtained. It is shown that the 31P nuclear magnetic resonance spectra of a number of nucleotide-enzyme complexes show some common features. In particular, the chemical shift values of the beta-phosphorus resonance of enzyme-bound NTP and NDP (N = A, G) of hydrolases exhibit a downfield shift virtually identical for myosin, elongation factor Tu, and the Ha-ras oncogene product p21. This suggests that the stereochemistry around the beta-phosphorus might be similar in these compounds.