Go to content
UR Home

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

Spoerner, Michael, Nuehs, Andrea, Herrmann, Christian, 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.

Full text not available from this repository.

at PubMed

at publisher (via DOI)


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 ...

plus


Export bibliographical data



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
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Item ID:16653
Owner only: item control page
  1. Homepage UR

University Library

Publication Server

Contact:

Publishing: oa@ur.de

Dissertations: dissertationen@ur.de

Research data: daten@ur.de

Contact persons