%0 Journal Article %1 opella_nmr_1997 %A Opella, S J %D 1997 %J Nat. Struct. Biol. %K Biomolecular,Lipid Conformation,Structural Magnetic Proteins,Micelles,Models,Nuclear Resonance,Phosphatidylcholines,Protein bilayers,Membrane %P 845--848 %T \NMR\ and membrane proteins %V 4 Suppl %X Membrane proteins are the next frontier for structural biology. It is feasible to determine the structures of smaller membrane proteins in micelles with solution NMR methods. However, it is the ability of solid-state NMR experiments to give completely resolved spectra of immobile proteins that enables the structures of larger membrane proteins to be determined in the definitive environment of lipid bilayers.

@article{opella_nmr_1997, abstract = {Membrane proteins are the next frontier for structural biology. It is feasible to determine the structures of smaller membrane proteins in micelles with solution NMR methods. However, it is the ability of solid-state NMR experiments to give completely resolved spectra of immobile proteins that enables the structures of larger membrane proteins to be determined in the definitive environment of lipid bilayers.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2e117b3b892c119af5cb360c3d8552941/nmrresource}, interhash = {2126337f5db9d5c07e7cc76128363606}, intrahash = {e117b3b892c119af5cb360c3d8552941}, issn = {1072-8368}, journal = {Nat. Struct. Biol.}, keywords = {Biomolecular,Lipid Conformation,Structural Magnetic Proteins,Micelles,Models,Nuclear Resonance,Phosphatidylcholines,Protein bilayers,Membrane}, month = oct, pages = {845--848}, pmid = {9377156}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{{\{}NMR{\}} and membrane proteins}}, volume = {4 Suppl}, year = 1997 }