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23296.0 [No comment] 28.06.2011 15:15 Released

ID: 23296.0, MPI für medizinische Forschung / Abteilung Biophysik
Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy
Translation of Title:Observation of slow dynamic exchange processes in Ras protein crystals by <sup>31</sup>P solid state NMR spectroscopy
Authors:Stumber, Michael; Geyer, Matthias; Graf, Robert; Kalbitzer, Hans Robert; Scheffzek, Klaus; Haeberlen, Ulrich
Date of Publication (YYYY-MM-DD):2002-11-08
Title of Journal:Journal of Molecular Biology
Journal Abbrev.:J. Mol. Biol.
Issue / Number:5
Start Page:899
End Page:907
Copyright:Copyright &copy; 2002 Elsevier Science Ltd.
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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 mm3 size single-crystal of GTPase Ras bound to the nucleotide GppNHp, that is, the signal from approximately 1015 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.
Free Keywords:solid state NMR; MAS NMR; protein dynamics; dynamics in crystals; Ras
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Forschungsgruppe Molekülkristalle
MPI für Polymerforschung
External Affiliations:Universität Regensburg, Institut für Biophysik und Physikalische Biochemie, Postfach, 93040, Regensburg, Germany; European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstraße 1, 69117, Heidelberg, Germany
Identifiers:URI:http://www.sciencedirect.com/science?_ob=ArticleUR... [Fulltext HTML]
URI:http://www.sciencedirect.com/science?_ob=ArticleUR... [Abstract]
URI:http://www.sciencedirect.com/science?_ob=MImg&_ima... [Fulltext PDF]