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Slow conformational dynamics of the guanine nucleotide-binding protein Ras complexed with the GTP analogue GTPγS

Spoerner, Michael and Nuehs, Andrea and Herrmann, Christian and Steiner, Guido and Kalbitzer, Hans Robert (2007) Slow conformational dynamics of the guanine nucleotide-binding protein Ras complexed with the GTP analogue GTPγS. The FEBS journal 274 (6), pp. 1419-1433.

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Abstract

The guanine nucleotide-binding protein Ras occurs in solution in two different conformational states, state 1 and state 2 with an equilibrium constant K(12) of 2.0, when the GTP analogue guanosine-5'-(beta,gamma-imido)triphosphate or guanosine-5'-(beta,gamma-methyleno)triphosphate is bound to the active centre. State 2 is assumed to represent a strong binding state for effectors with a ...

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Item Type:Article
Date:2007
Additional information (public):Nebent.: European journal of biochemistry
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
17302736PubMed ID
10.1111/j.1742-4658.2007.05681.xDOI
Classification:
NotationType
Guanosine 5'-O-(3-Thiotriphosphate)/metabolismMESH
Hydrogen-Ion ConcentrationMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Protein BindingMESH
Protein ConformationMESH
ThermodynamicsMESH
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 06:36
Last Modified:17 Sep 2010 06:36
Item ID:16653
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