Research Article

Quantitative measurement of differential 15N[BOND]Hα/βT2 relaxation rates in a perdeuterated protein by MAS solid-state NMR spectroscopy

  1. Veniamin Chevelkov1,
  2. Anne Diehl1,
  3. Bernd Reif1,2,*

Article first published online: 21 DEC 2007

DOI: 10.1002/mrc.2129

Issue

Magnetic Resonance in Chemistry

Magnetic Resonance in Chemistry

Special Issue: New techniques in solid-state NMR

Volume 45, Issue S1, pages S156–S160, December 2007

Additional Information

How to Cite

Chevelkov, V., Diehl, A. and Reif, B. (2007), Quantitative measurement of differential 15N[BOND]Hα/βT2 relaxation rates in a perdeuterated protein by MAS solid-state NMR spectroscopy. Magn. Reson. Chem., 45: S156–S160. doi: 10.1002/mrc.2129

Author Information

  1. 1

    Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle Str. 10, 13125, Berlin, Germany

  2. 2

    Charité Universitätsmedizin, D-10115, Berlin, Germany

*Charité Universitätsmedizin, D-10115, Berlin, Germany.

Publication History

  1. Issue published online: 21 DEC 2007
  2. Article first published online: 21 DEC 2007
  3. Manuscript Accepted: 28 SEP 2007
  4. Manuscript Revised: 19 SEP 2007
  5. Manuscript Received: 11 JUL 2007

Funded by

  • DFG. Grant Number: Re1435

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Keywords:

  • deuteration;
  • transverse relaxation;
  • CSA-dipole cross-correlated relaxation;
  • MAS solid-state NMR;
  • magic angle spinning;
  • protein micro-crystals

Abstract

Dynamic parameters become more and more accessible in the study of uniformly isotopically enriched proteins by MAS solid-state NMR. We demonstrate that T2-related relaxation properties can quantitatively be determined in a sample of a perdeuterated microcrystalline protein by the measurement of 15N,1H dipole, 15N CSA cross-correlated relaxation rates. We find that the measured cross-correlated relaxation rates are independent of the MAS rotation frequency, and therefore reflect local dynamic fluctuations of the protein structure. Copyright © 2007 John Wiley & Sons, Ltd.

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