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31P−NMR spectra of the Ha−ras p21. Nucleotide complexes

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons95056

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95966

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95288

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

http://pubman.mpdl.mpg.de/cone/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;

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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: http://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 −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 −phosphorus might be similar in these compoun