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Solution NMR of membrane proteins: practice and challenges

  1. Charles R. Sanders1,*,
  2. Frank Sönnichsen2,*

Article first published online: 6 JUL 2006

DOI: 10.1002/mrc.1816

Issue

Magnetic Resonance in Chemistry

Magnetic Resonance in Chemistry

Special Issue: NMR of Proteins in Solution

Volume 44, Issue S1, pages S24–S40, July 2006

Additional Information

How to Cite

Sanders, C. R. and Sönnichsen, F. (2006), Solution NMR of membrane proteins: practice and challenges. Magn. Reson. Chem., 44: S24–S40. doi: 10.1002/mrc.1816

Author Information

  1. 1

    Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232-8725, USA

  2. 2

    Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA

*Department of Biochemistry, Vanderbilt University, Nashville, TN 37232.

Publication History

  1. Issue published online: 6 JUL 2006
  2. Article first published online: 6 JUL 2006
  3. Manuscript Accepted: 28 FEB 2006
  4. Manuscript Revised: 25 JAN 2006
  5. Manuscript Received: 2 DEC 2005

Funded by

  • US NIH PO1 GM64676
  • RO1 GM47485

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Keywords:

  • NMR;
  • membrane;
  • proteins;
  • solution;
  • review;
  • detergent;
  • detergents;
  • micelles;
  • amphipols;
  • lipopeptides;
  • bicelles;
  • TROSY;
  • labeling;
  • deuteration;
  • structure;
  • backbone;
  • fold

Abstract

This review focuses upon the application of solution NMR methods to multispan integral membrane proteins, particularly with respect to determination of global folds by this approach. Practical methods are described along with the special difficulties that confront the application of solution NMR to proteins that dwell in the netherworld of the lipid bilayer. Copyright © 2006 John Wiley & Sons, Ltd.

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