title: Membrane protein structure determination: back to the membrane.
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.
authors: Sanford Burnham Medical Research Institute, La Jolla, CA, USA.
authors: Yong
authors: Y
authors: Yao
authors: Yi
authors: Y
authors: Ding
authors: Ye
authors: Y
authors: Tian
authors: Stanley J
authors: SJ
authors: Opella
authors: Francesca M
authors: FM
authors: Marassi
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002462:Cell Membrane / Q000737:chemistry*; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008051:Lipid Bilayers / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D015010:Yersinia pestis
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; C482905:OmpX protein, E coli; D006867:Hydrolases
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