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  Observation of slow dynamic exchange processes in Ras protein crystals by 31P 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 31P solid state NMR spectroscopy. Journal of Molecular Biology (London), 323(5), 899-907. doi:10.1016/S0022-2836(02)01010-0.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7C1C-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7C1D-9
Genre: Journal Article
Alternative Title : Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy

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JMolBiol_323_2002_899.pdf (Any fulltext), 856KB
 
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 Creators:
Stumber, Michael1, Author              
Geyer, Matthias2, Author              
Graf, Robert, Author
Kalbitzer, Hans Robert2, Author              
Scheffzek, Klaus2, Author              
Haeberlen, Ulrich1, Author              
Affiliations:
1Research Group Prof. Dr. Haeberlen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497739              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: solid state NMR; MAS NMR; protein dynamics; dynamics in crystals; Ras
 Abstract: 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 0.3mm(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.

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Language(s): eng - English
 Dates: 2002-08-202002-06-122002-08-272002-10-292002-11-08
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 323 (5) Sequence Number: - Start / End Page: 899 - 907 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042