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Perturbation of the conformational equilibria in Ras by selective mutations as studied by ³¹P NMR spectroscopy

Spoerner, Michael and Wittinghofer, Alfred and Kalbitzer, Hans Robert (2004) Perturbation of the conformational equilibria in Ras by selective mutations as studied by ³¹P NMR spectroscopy. FEBS letters 578 (3), pp. 305-310.

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Abstract

Ras regulates a variety of different signal transduction pathways acting as molecular switch. It was shown by liquid and solid-state (31)P NMR spectroscopy that Ras exists in the guanosine-5'-(beta,gamma-imido)triphosphate bound form in at least two conformational states interconverting in millisecond time scale. The relative population between the two conformational states affects drastically ...

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Item Type:Article
Date:2004
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
15589837PubMed ID
10.1016/j.febslet.2004.11.020DOI
Classification:
NotationType
Amino Acid SequenceMESH
Amino Acid SubstitutionMESH
Escherichia coli/geneticsMESH
GTPase-Activating Proteins/metabolismMESH
Genes, rasMESH
Genetic VariationMESH
Guanosine Diphosphate/metabolismMESH
HumansMESH
Hydrogen-Ion ConcentrationMESH
KineticsMESH
Models, MolecularMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Phosphorus/chemistryMESH
Phosphorus IsotopesMESH
Point MutationMESH
Protein BindingMESH
Protein ConformationMESH
Protein Structure, TertiaryMESH
Signal TransductionMESH
TemperatureMESH
Threonine/metabolismMESH
ras Proteins/metabolismMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:17 Sep 2010 06:30
Last Modified:17 Sep 2010 06:30
Item ID:16622
Owner Only: item control page
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