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  Observation of slow dynamic exchange processes in Ras protein crystals by P-31 solid state NMR spectroscopy

Stumber, M., Geyer, M., Graf, R., Kalbitzer, H. R., Scheffzek, K., & Haeberlen, U. (2002). Observation of slow dynamic exchange processes in Ras protein crystals by P-31 solid state NMR spectroscopy. Journal of Molecular Biology, 323(5), 899-907.

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Stumber, M., Autor
Geyer, M., Autor
Graf, Robert1, Autor           
Kalbitzer, H. R., Autor
Scheffzek, K., Autor
Haeberlen, U., Autor
Affiliations:
1MPI for Polymer Research, Max Planck Society, ou_1309545              

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Schlagwörter: solid state NMR; MAS NMR; protein dynamics; dynamics in crystals; Ras
 Zusammenfassung: The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein crystallization, leading, in X-ray diffraction experiments, to a blurring of the electron density map and reducing the resolution of the derived structure. Nuclear magnetic resonance (NMR) is known to be an alternative method to study molecular structure and dynamics. We designed and built a probe for phosphorus solid state NMR that allows for the first time to study static properties as well as dynamic processes in single-crystals of a protein by NMR spectroscopy. The sensitivity achieved is sufficient to detect the NMR signal from individual phosphorus sites in a 0.3 mm(3) size single- crystal of GTPase Ras bound to the nucleotide GppNHp, that is, the signal from approximately 10(15) phosphorus nuclei. The NMR spectra obtained are discussed in terms of the conformational variability of the active center of the Ras-nucleotide complex. We conclude that, in the crystal, the protein complex exists in three different conformations. Magic angle spinning (MAS) NMR spectra of a powder sample of Ras-GppNHp show a splitting of one of the phosphate resonances and thus confirm this conclusion. The MAS spectra provide, furthermore, evidence of a slow, temperature-dependent dynamic exchange process in the Ras protein crystal. (C) 2002 Elsevier Science Ltd. All rights reserved.

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Sprache(n): eng - English
 Datum: 2002-11-08
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Keine Begutachtung
 Identifikatoren: eDoc: 28453
ISI: 000179308500010
Anderer: P-02-155
 Art des Abschluß: -

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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 323 (5) Artikelnummer: - Start- / Endseite: 899 - 907 Identifikator: ISSN: 0022-2836