Abstract
The growing need for structure determination of membrane proteins incorporated within their native bilayers calls for the development of novel experimental methods and membrane mimetics for the structure-function studies of these important biological constituents. Solid-state NMR of macroscopically aligned samples has emerged as a powerful tool that enables studies of membrane proteins under their native-like conditions. Here we present an alternative alignment method based on anodic aluminum oxide nanopores, which are capable of incorporating a broad repertoire of lipids. Moreover, the temperature and pH stability of lipid bilayers within the nanopores enable solid-state NMR experiments under a wider range of conditions than ever before. Uniaxial motional averaging by rotational diffusion of membrane proteins ensures the line narrowing of experimental NMR linewidths, thus, providing structural and dynamic information for the lipid-embedded proteins.
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Acknowledgements
The assistance of Dr. Antonin Marek (NCSU) in the preparation of Fig. 7 is gratefully acknowledged. The fabrication of AAO and development of lipid nanotube technology for lipid bilayers and membrane proteins was supported by US DOE Contract DE-FG02-02ER15354 to AIS. OS NMR experiments were supported by NSF MRI 1229547 to AAN.
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Nevzorov, A., Smirnov, A. (2015). Line Narrowing in Oriented-Sample NMR of Membrane Proteins. In: Berliner, L. (eds) Protein NMR. Biological Magnetic Resonance, vol 32. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-7621-5_5
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