Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins. J Magn Reson 2003 Mar;161(1):64-9
Date
03/28/2003Pubmed ID
12660112Pubmed Central ID
PMC3033728DOI
10.1016/s1090-7807(02)00182-9Scopus ID
2-s2.0-0042994281 (requires institutional sign-in at Scopus site) 34 CitationsAbstract
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.
Author List
Marassi FM, Crowell KJAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnisotropyLipid Bilayers
Magnetic Resonance Spectroscopy
Membrane Proteins
Phospholipids
Protein Conformation
