Review

Solution NMR methods for quantitative identification of chemical exchange in 15N-labeled proteins

  1. Chunyu Wang,
  2. Arthur G. Palmer III*

Article first published online: 9 SEP 2003

DOI: 10.1002/mrc.1262

Issue

Magnetic Resonance in Chemistry

Magnetic Resonance in Chemistry

Special Issue: Relaxation in NMR

Volume 41, Issue 10, pages 866–876, October 2003

Additional Information

How to Cite

Wang, C. and Palmer, A. G. (2003), Solution NMR methods for quantitative identification of chemical exchange in 15N-labeled proteins. Magn. Reson. Chem., 41: 866–876. doi: 10.1002/mrc.1262

Author Information

  1. Department of Biochemistry and Molecular Biophysics, Columbia University, 630 W. 168th Street, New York, NY10032, USA

*Department of Biochemistry and Molecular Biophysics, Columbia University, 630 W. 168th Street, New York, NY 10032, USA.

Publication History

  1. Issue published online: 9 SEP 2003
  2. Article first published online: 9 SEP 2003
  3. Manuscript Revised: 23 JUN 2003
  4. Manuscript Accepted: 23 JUN 2003
  5. Manuscript Received: 28 APR 2003

Funded by

  • NIH. Grant Numbers: DK07328, GM59273, GM66354.

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Keywords:

  • chemical exchange;
  • protein dynamics;
  • cross correlation;
  • TROSY;
  • CPMG;
  • transverse relaxation

Abstract

Chemical exchange phenomena in NMR spectra reveal protein motions on microsecond to millisecond time scales that are associated with biological functions, including catalysis, ligand binding, allosteric conformational changes and protein folding. This review surveys solution NMR methods for identifying chemical exchange in proteins by measuring transverse relaxation rate constants for backbone 15N spins. The relaxation-compensated-IzSz and in-phase Hahn echo methods are suitable for small- to medium-sized proteins. The transverse relaxation optimized spectroscopy method is suitable for large, deuterated proteins. Differential multiple quantum relaxation is also a signature of chemical exchange and provides unique information about exchange processes. The various methods are illustrated by application to basic pancreatic trypsin inhibitor and triosephosphate isomerase. Copyright © 2003 John Wiley & Sons, Ltd.

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