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Conformational states of Ras complexed with the GTP analogue GppNHp or GppCH₂p: implications for the interaction with effector proteins

Spoerner, Michael and Nuehs, Andrea and Ganser, Petra and Herrmann, Christian and Wittinghofer, Alfred and Kalbitzer, Hans Robert (2005) Conformational states of Ras complexed with the GTP analogue GppNHp or GppCH₂p: implications for the interaction with effector proteins. Biochemistry 44 (6), pp. 2225-2236.

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Abstract

The guanine nucleotide-binding protein Ras occurs in solution in two different states, state 1 and state 2, when the GTP analogue GppNHp is bound to the active center as detected by (31)P NMR spectroscopy. Here we show that Ras(wt).Mg(2+).GppCH(2)p also exists in two conformational states in dynamic equilibrium. The activation enthalpy DeltaH(++)(12) and the activation entropy DeltaS(++)(12) for ...

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Item Type:Article
Date:2005
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
15697248PubMed ID
10.1021/bi0488000DOI
Classification:
NotationType
Amino Acid Substitution/geneticsMESH
Cations, Divalent/chemistryMESH
Deuterium Exchange MeasurementMESH
Guanosine Triphosphate/metabolismMESH
Guanylyl Imidodiphosphate/metabolismMESH
HumansMESH
KineticsMESH
Magnesium/chemistryMESH
Magnetic Resonance Spectroscopy/methodsMESH
Phosphates/metabolismMESH
Phosphorus Isotopes/metabolismMESH
Protein BindingMESH
Protein ConformationMESH
Proto-Oncogene Proteins c-raf/metabolismMESH
ThermodynamicsMESH
ral Guanine Nucleotide Exchange Factor/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 06:32
Last Modified:17 Sep 2010 06:32
Item ID:16624
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