ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2003
Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 32 citations in OpenAlex.
- Contributions and Limitations of Biophysical Approaches to Study of the Interactions between Amphiphilic Molecules and the Plant Plasma Membrane.Plants (Basel, Switzerland) · 2020Review
- Investigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study.Biophysical journal · 2007Article
- Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2007Article
- Flow-through lipid nanotube arrays for structure-function studies of membrane proteins by solid-state NMR spectroscopy.Biophysical journal · 2006Article
- Optimizing oriented planar-supported lipid samples for solid-state protein NMR.Biophysical journal · 2005Article
- Structural studies of apoptosis and ion transport regulatory proteins in membranes.Magnetic resonance in chemistry : MRC · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The preparation of oriented, hydration-optimized lipid bilayer samples, for NMR structure determination of membrane proteins, is described. The samples consist of planar phospholipid bilayers, containing membrane proteins, that are oriented on single pairs of glass slides, and are placed in the coil of the NMR probe with the bilayer plane perpendicular to the direction of the magnetic field. Lipid bilayers provide a medium that closely resembles the biological membrane, and sample orientation both preserves the intrinsic membrane-defined directional quality of membrane proteins, and provides the mechanism for resonance line narrowing. The hydration-optimized samples overcome some of the difficulties associated with multi-dimensional, high-resolution, solid-state NMR spectroscopy of membrane proteins. These samples have greater stability over the course of multi-dimensional NMR experiments, they have lower sample conductance for greater rf power efficiency, and enable greater rf coil filling factors to be obtained for improved experimental sensitivity. Sample preparation is illustrated for the membrane protein CHIF (channel inducing factor), a member of the FXYD family of ion transport regulators.
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