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Solid-state 31P NMR of nucleotide binding proteins

URN to cite this document: urn:nbn:de:bvb:355-opus-4432

Iuga, Adriana (2004) Solid-state 31P NMR of nucleotide binding proteins. PhD, Universität Regensburg.

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Abstract (English)

The major results of the present work are related to low molecular weight guanosine triphosphate (GTP) binding Ras proteins which play an essential role in a variety of diverse cellular signal transduction and transport processes by cycling between a GTP-bound �on� state and a guanosine diphosphate (GDP) bound �off� state. Ras(wt)·Mg2+·GppNHp exists in two biological relevant conformational ...


Translation of the abstract (German)

Das Guaninnukleotid-bindende Protein Ras ist als molekularer Schalter in zellulären Signaltransduktionswegen involviert. Ras(wt) kann in der aktiven Konformation in zwei konformationellen Zuständen vorliegen (Zustand 1 und 2), die sich im chemischen Austausch miteinander befinden. Das Gleichgewicht zwischen den beiden Zuständen wird durch Mutationen in der Schalter I-Region von Ras zum Zustand 1 ...


Export bibliographical data

Item type:Thesis of the University of Regensburg (PhD)
Date:20 December 2004
Referee:Eike (Prof. Dr.) Brunner
Date of exam:7 December 2004
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner
Keywords:Ras-Proteine , Festkörper-NMR-Spektroskopie , Molekulardynamik , , Ras protein , conformational exchange , solid-state 31P NMR
Dewey Decimal Classification:500 Science > 570 Life sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Deposited on:26 Oct 2009 15:38
Last modified:13 Mar 2014 11:25
Item ID:10243
Owner only: item control page


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