Document Type
Article
Publication Date
4-2012
Source Publication
Biomolecular NMR Assignments
Source ISSN
1874-2718
Abstract
The small GTPase Ras is an important signaling molecule acting as a molecular switch in eukaryotic cells. Recent findings of global conformational exchange and a putative allosteric binding site in the G domain of Ras opened an avenue to understanding novel aspects of Ras function. To facilitate detailed NMR studies of Ras in physiological solution conditions, we performed backbone resonance assignments of Ras bound to slowly hydrolysable GTP mimic, guanosine 5′-[ß, γ-imido]triphosphate at pH 7.2. Out of 163 non-proline residues of the G domain, signals from backbone amide proton, nitrogen and carbon spins of 127 residues were confidently assigned with the remaining unassigned residues mostly located at the exchange-broadened effectors interface.
Recommended Citation
O'Connor, Casey and Kovriguine, Evgueni, "Assignments of backbone 1H, 13C and 15N resonances in H-Ras (1–166) complexed with GppNHp at physiological pH" (2012). Chemistry Faculty Research and Publications. 246.
https://epublications.marquette.edu/chem_fac/246
Comments
Accepted version. Biomolecular NMR Assignments, Vol. 6, No. 1 (April 2012) 91-93. DOI: 10.1007/s12104-011-9332-3. © 2012 Springer Nature Switzerland AG. Part of Springer Nature. Used with permission.
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