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Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and ³¹P NMR spectroscopy

Rohrer, M. and Prisner, T. F. and Brügmann, O. and Käss, H. and Spoerner, M. and Wittinghofer, A. and Kalbitzer, Hans Robert (2001) Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and ³¹P NMR spectroscopy. Biochemistry 40 (7), pp. 1884-1889.

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Abstract

The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of the metal ion in the inactive, GDP-bound Ras has been studied by continuous wave EPR at 94 GHz (W-band). Via replacement of normal water with (17)O-enriched water, the (17)O--(55)Mn superhyperfine coupling was used to determine ...

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Item Type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
11329253PubMed ID
10.1021/bi002164yDOI
Classification:
NotationType
Amino Acid Substitution/geneticsMESH
Electron Spin Resonance Spectroscopy/methodsMESH
Guanosine Diphosphate/chemistryMESH
Macromolecular SubstancesMESH
Manganese/chemistryMESH
Mutagenesis, Site-DirectedMESH
Nuclear Magnetic Resonance, Biomolecular/methodsMESH
Point MutationMESH
SolutionsMESH
TemperatureMESH
Water/chemistryMESH
ras Proteins/geneticsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:02
Last Modified:15 Sep 2010 09:02
Item ID:16574
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