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Solid-state ³¹P NMR spectroscopy of microcrystals of the Ras protein and its effector loop mutants: comparison between crystalline and solution state

Iuga, Adriana and Spoerner, Michael and Kalbitzer, Hans Robert and Brunner, Eike (2004) Solid-state ³¹P NMR spectroscopy of microcrystals of the Ras protein and its effector loop mutants: comparison between crystalline and solution state. Journal of molecular biology 342 (3), pp. 1033-1040.

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Abstract

Cycling between a GTP bound "on" state and a GDP bound "off" state, guanine nucleotide-binding (GNB) proteins act as molecular switches. The switching process and the interaction with effectors, GTPase-activating proteins, and guanosine nucleotide-exchange factors is accompanied by pronounced conformational changes of the switch regions of the GNB proteins. The aim of the present contribution is ...

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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
15342254PubMed ID
10.1016/j.jmb.2004.07.077DOI
Classification:
NotationType
Binding SitesMESH
CrystallizationMESH
Guanosine Diphosphate/metabolismMESH
Guanosine Triphosphate/metabolismMESH
Guanylyl Imidodiphosphate/metabolismMESH
Models, MolecularMESH
Mutagenesis, Site-DirectedMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Phosphorus/chemistryMESH
Protein ConformationMESH
Recombinant Proteins/metabolismMESH
SolutionsMESH
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:16 Sep 2010 09:27
Last Modified:16 Sep 2010 09:27
Item ID:16610
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