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Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR
Author(s) -
Tamm Lukas K,
Abildgaard Frits,
Arora Ashish,
Blad Heike,
Bushweller John H
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01127-x
Subject(s) - hemagglutinin (influenza) , nuclear magnetic resonance spectroscopy , micelle , chemistry , biophysics , membrane protein , influenza a virus , lipid bilayer fusion , viral membrane , function (biology) , membrane , nuclear magnetic resonance , biochemistry , biology , virus , microbiology and biotechnology , physics , virology , stereochemistry , viral envelope , glycoprotein , aqueous solution , gene
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles by solution nuclear magnetic resonance (NMR) is reviewed. NMR opens a new window to also study, for the first time, the dynamics of membrane proteins. We report on recent attempts to correlate dynamic measurements on OmpA with the ion channel function of this protein. We also summarize how NMR and spin‐label electron paramagnetic resonance spectroscopy and selective mutagenesis can be combined to provide a structural basis towards understanding the mechanism of influenza hemagglutinin‐mediated membrane fusion.