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Membrane Protein Structure Determination: Back to the Membrane

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Membrane Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1063))

Abstract

NMR spectroscopy enables the structures of membrane proteins to be determined in the native-like environment of the phospholipid bilayer membrane. This chapter outlines the methods for membrane protein structural studies using solid-state NMR spectroscopy with samples of membrane proteins incorporated in proteoliposomes or planar lipid bilayers. The methods for protein expression and purification, sample preparation, and NMR experiments are described and illustrated with examples from OmpX and Ail, two bacterial outer membrane proteins that function in bacterial virulence.

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Acknowledgments

This research was supported by grants from the National Institutes of Health (R21 GM075917; R21 GM094727; R01 GM100265). The NMR studies utilized the NMR Facility at Sanford-Burnham Medical Research Institute, and the Resource for Molecular Imaging of Proteins at UCSD, each supported by grants from the National Institutes of Health (P30 CA030199; P41 EB002031).

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Authors and Affiliations

  1. Sanford Burnham Medical Research Institute, La Jolla, CA, USA

    Yong Yao, Yi Ding, Ye Tian & Francesca M. Marassi

  2. Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA

    Ye Tian & Stanley J. Opella

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  1. Yong Yao
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  2. Yi Ding
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  3. Ye Tian
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  4. Stanley J. Opella
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  5. Francesca M. Marassi
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Editors and Affiliations

  1. Dept. of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, USA

    Giovanna Ghirlanda

  2. Department of Biochemistry, University of Wisconsin, Madison, Madison, Wisconsin, USA

    Alessandro Senes

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Yao, Y., Ding, Y., Tian, Y., Opella, S.J., Marassi, F.M. (2013). Membrane Protein Structure Determination: Back to the Membrane. In: Ghirlanda, G., Senes, A. (eds) Membrane Proteins. Methods in Molecular Biology, vol 1063. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-583-5_8

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  • DOI: https://doi.org/10.1007/978-1-62703-583-5_8

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