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NMR structures of membrane proteins in phospholipid bilayers

Published online by Cambridge University Press:  17 July 2014

Jasmina Radoicic ,
George J. Lu  and
Stanley J. Opella
Jasmina Radoicic
Affiliation:
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA
George J. Lu
Affiliation:
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA
Stanley J. Opella*
Affiliation:
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA
*
*Author for correspondence: S. J. Opella, Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA. Tel.: 858 822-4820; Email: sopella@ucsd.edu
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Abstract

Membrane proteins have always presented technical challenges for structural studies because of their requirement for a lipid environment. Multiple approaches exist including X-ray crystallography and electron microscopy that can give significant insights into their structure and function. However, nuclear magnetic resonance (NMR) is unique in that it offers the possibility of determining the structures of unmodified membrane proteins in their native environment of phospholipid bilayers under physiological conditions. Furthermore, NMR enables the characterization of the structure and dynamics of backbone and side chain sites of the proteins alone and in complexes with both small molecules and other biopolymers. The learning curve has been steep for the field as most initial studies were performed under non-native environments using modified proteins until ultimately progress in both techniques and instrumentation led to the possibility of examining unmodified membrane proteins in phospholipid bilayers under physiological conditions. This review aims to provide an overview of the development and application of NMR to membrane proteins. It highlights some of the most significant structural milestones that have been reached by NMR spectroscopy of membrane proteins, especially those accomplished with the proteins in phospholipid bilayer environments where they function.

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Review Article
Information
Quarterly Reviews of Biophysics , Volume 47 , Issue 3 , August 2014 , pp. 249 - 283
Copyright
Copyright © Cambridge University Press 2014 

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