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M2 Proton Channel Structural Validation from Full‐Length Protein Samples in Synthetic Bilayers and E. coli Membranes
Author(s) -
Miao Yimin,
Qin Huajun,
Fu Riqiang,
Sharma Mukesh,
Can Thach V.,
Hung Ivan,
Luca Sorin,
Gor'kov Peter L.,
Brey William W.,
Cross Timothy A.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201204666
Subject(s) - membrane , lipid bilayer , characterization (materials science) , chemistry , membrane protein , bilayer , biophysics , analytical chemistry (journal) , materials science , biochemistry , chromatography , nanotechnology , biology
Validation : Membrane protein structures are sensitive to the environment used for structural characterization. NMR spectra of the full‐length M2 proton channel from influenza A were measured directly in E. coli membranes and compared to spectra of the protein in synthetic lipid bilayers. The results demonstrate that these bilayers provide a native‐like membrane environment.