Membrane protein structure determination: back to the membrane

Methods Mol Biol. 2013:1063:145-58. doi: 10.1007/978-1-62703-583-5_8.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / isolation & purification
  • Cell Membrane / chemistry*
  • Crystallography, X-Ray
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / isolation & purification
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / isolation & purification
  • Lipid Bilayers / chemistry
  • Models, Molecular*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Yersinia pestis

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • Lipid Bilayers
  • OmpX protein, E coli
  • Hydrolases