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

P. Rösch; A. Wittinghofer; J. Tucker; G. Sczakiel; R. Leberman; I. Schlichting

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

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

P. Rösch^*, A. Wittinghofer, J. Tucker, G. Sczakiel, R. Leberman, I. Schlichting

^*Korrespondierende/r Autor/-in für diese Arbeit

18 Zitate (Scopus)

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 β-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 β-phosphorus might be similar in these compounds.

Originalsprache	Englisch
Zeitschrift	Biochemical and Biophysical Research Communications
Jahrgang	135
Ausgabenummer	2
Seiten (von - bis)	549-555
Seitenumfang	7
ISSN	0006-291X
DOIs	https://doi.org/10.1016/0006-291X(86)90029-X
Publikationsstatus	Veröffentlicht - 13.03.1986

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

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title = "31P-NMR spectra of the Ha-ras p21. Nucleotide complexes",

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 β-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 β-phosphorus might be similar in these compounds.",

author = "P. R{\"o}sch and A. Wittinghofer and J. Tucker and G. Sczakiel and R. Leberman and I. Schlichting",

year = "1986",

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T1 - 31P-NMR spectra of the Ha-ras p21. Nucleotide complexes

AU - Rösch, P.

AU - Wittinghofer, A.

AU - Tucker, J.

AU - Sczakiel, G.

AU - Leberman, R.

AU - Schlichting, I.

PY - 1986/3/13

Y1 - 1986/3/13

N2 - 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 β-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 β-phosphorus might be similar in these compounds.

AB - 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 β-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 β-phosphorus might be similar in these compounds.

UR - https://www.scopus.com/pages/publications/0022558155

U2 - 10.1016/0006-291X(86)90029-X

DO - 10.1016/0006-291X(86)90029-X

M3 - Journal articles

C2 - 3485974

AN - SCOPUS:0022558155

SN - 0006-291X

VL - 135

SP - 549

EP - 555

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

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