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.
%0 Journal Article
%1 yao_membrane_2013
%A Yao, Yong
%A Ding, Yi
%A Tian, Ye
%A Opella, Stanley J
%A Marassi, Francesca M
%D 2013
%J Methods Mol. Biol.
%K Bacterial Conformation,X-Ray,Yersinia Magnetic Membrane Membrane,Crystallography,Escherichia Outer Proteins,Biomolecular,Cell Proteins,Hydrolases,Lipid Resonance,Protein bilayers,Models,Molecular,Nuclear coli pestis
%P 145--158
%R 10.1007/978-1-62703-583-5_8
%T Membrane protein structure determination: back to the membrane
%V 1063
%X 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.
@article{yao_membrane_2013,
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.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Yao, Yong and Ding, Yi and Tian, Ye and Opella, Stanley J and Marassi, Francesca M},
biburl = {https://www.bibsonomy.org/bibtex/29fbddd92d2279c60482e74b69800f8a9/nmrresource},
doi = {10.1007/978-1-62703-583-5_8},
interhash = {dabb3f63ec46676edafc4a1adc9591e3},
intrahash = {9fbddd92d2279c60482e74b69800f8a9},
issn = {1940-6029},
journal = {Methods Mol. Biol.},
keywords = {Bacterial Conformation,X-Ray,Yersinia Magnetic Membrane Membrane,Crystallography,Escherichia Outer Proteins,Biomolecular,Cell Proteins,Hydrolases,Lipid Resonance,Protein bilayers,Models,Molecular,Nuclear coli pestis},
pages = {145--158},
pmid = {23975776},
shorttitle = {Membrane protein structure determination},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Membrane protein structure determination: back to the membrane}},
volume = 1063,
year = 2013
}