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Journal Article

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

MPS-Authors
/persons/resource/persons95056

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

/persons/resource/persons95966

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

/persons/resource/persons95288

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

/persons/resource/persons95189

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

External Resource

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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Citation

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.


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