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Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5'-triphosphate hydrolysis of p21ras

Schweins, T. and Geyer, M. and Kalbitzer, Hans Robert and Wittinghofer, A. and Warshel, A. (1996) Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5'-triphosphate hydrolysis of p21ras. Biochemistry 35 (45), pp. 14225-14231.

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Abstract

Controlling the hydrolysis rate of GTP bound to guanine nucleotide binding proteins is crucial for the right timing of many biological processes. Theoretical, structural, and functional studies have demonstrated that in p21ras the substrate of the reaction, GTP itself, plays a central role by acting as the base catalyst. This substrate-assisted reaction mechanism was analyzed with the help of ...

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Item Type:Article
Date:1996
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
8916907PubMed ID
10.1021/bi961118oDOI
Classification:
NotationType
Binding SitesMESH
Enzyme ActivationMESH
GTP Phosphohydrolases/metabolismMESH
GTPase-Activating ProteinsMESH
Guanosine Triphosphate/metabolismMESH
HumansMESH
KineticsMESH
Mutagenesis, Site-DirectedMESH
Protein BindingMESH
Proteins/metabolismMESH
Proto-Oncogene Proteins p21(ras)/metabolismMESH
Recombinant ProteinsMESH
Structure-Activity RelationshipMESH
ThermodynamicsMESH
ras GTPase-Activating ProteinsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:22
Last Modified:13 Sep 2010 08:22
Item ID:16546
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