Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR Export

@article{citeulike:2827016, abstract = {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.}, author = {Tamm, Lukas K. and Abildgaard, Frits and Arora, Ashish and Blad, Heike and Bushweller, John H.}, booktitle = {126th Nobel Symposium. Membrane Proteins: Structure, Function and Assembly}, citeulike-article-id = {2827016}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0014-5793(03)01127-X}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6T36-49PYH7S-M/1/beaf767e7445c316b8090d94675401a5}, day = {27}, doi = {10.1016/S0014-5793(03)01127-X}, journal = {FEBS Letters}, keywords = {dynamics, imp, model-free, structure}, month = {November}, number = {1}, pages = {139--143}, posted-at = {2008-05-23 22:08:39}, priority = {0}, title = {Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR}, url = {http://dx.doi.org/10.1016/S0014-5793(03)01127-X}, volume = {555}, year = {2003} }

TY - JOUR ID - citeulike:2827016 L3 - citeulike-article-id:2827016 N2 - 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. IS - 1 JF - FEBS Letters EP - 143 TI - Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR VL - 555 T2 - 126th Nobel Symposium. Membrane Proteins: Structure, Function and Assembly SP - 139 KW - dynamics KW - imp KW - model-free KW - structure AU - Tamm, Lukas AU - Abildgaard, Frits AU - Arora, Ashish AU - Blad, Heike AU - Bushweller, John PY - 2003/11/27/ UR - http://dx.doi.org/10.1016/S0014-5793(03)01127-X ER -