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The application of magic angle sample spinning (MAS) NMR to uniformly aligned biomembrane samples is demonstrated as a new general approach toward structural studies of membrane proteins, peptides, and lipids. The spectral linewidth from a multilamellar lipid dispersion is dominated, in the case of protons, by the dipolar coupling. For low-gamma or dilute spins, however, the chemical shift anisotropy dominates the spectral linewidth, which is reduced by the two-dimensional order in a uniformly aligned lipid membrane. The remaining line broadening, which is due to orientational defects ("mosaic spread") can be easily removed at low spinning speeds. This orientational order in the sample also allows the anisotropic intermolecular motions of membrane components (such as rotational diffusion, tauc = 10(-10) s) for averaging dipolar interactions to be utilized, e.g., by placing the membrane normal parallel to the rotor axis. The dramatic resolution improvement for protons which are achieved in a lipid sample at only 220 Hz spinning speed in a 9.4 T field is slightly better than any data published to date using ultra-high fields (up to 17.6 T) and high-speed spinning (14 kHz). Additionally, the analysis of spinning sidebands provides valuable orientational information. We present the first 1H, 31P, and 13C MAS spectra of uniformly aligned dimyristoylphosphatidylcholine (DMPC) bilayers. Also, 1H resolution enhancement for the aromatic region of the M13 coat protein reconstituted into DMPC bilayers is presented. This new method combines the high resolution usually achieved by MAS with the advantages of orientational constraints obtained by working with macroscopically oriented samples. We describe the general potential and possible perspectives of this technique.

Original publication

DOI

10.1006/jmre.1997.1344

Type

Journal article

Journal

J Magn Reson

Publication Date

02/1998

Volume

130

Pages

305 - 316

Keywords

Anisotropy, Computer Simulation, Dimyristoylphosphatidylcholine, Image Processing, Computer-Assisted, Membranes, Artificial, Molecular Structure, Nuclear Magnetic Resonance, Biomolecular