Structure determination of aligned systems by solid-state NMR magic angle spinning methods.

Benjamin J Gross; Joseph M Tanski; Ann E McDermott

doi:10.1016/j.jmr.2005.06.008

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Structure determination of aligned systems by solid-state NMR magic angle spinning methods.

Benjamin J Gross·Joseph M Tanski·Ann E McDermott

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Abstract

Single crystal rotational echo double resonance (REDOR) experiments can be used to determine the three-dimensional orientation of heteronuclear bond vectors in an amino acid, as well as the crystal's orientation relative to the rotor fixed frame (RFF). We also demonstrate that for samples uniaxially aligned along the rotor axis, the polar tilt angle of a bond vector relative to the RFF can be measured by use of an analytical expression that describes the REDOR curve for that system. These bond orientations were verified by X-ray indexing of the single crystal sample, and were shown to be as accurate as +/- 1 degrees .

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Alanine Algorithms Anisotropy Computer Simulation Crystallography Magnetic Resonance Spectroscopy Models, Chemical Models, Molecular Molecular Conformation Phase Transition Powders Rotation Spin Labels Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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Benjamin J Gross, Joseph M Tanski, Ann E McDermott. 2005. Structure determination of aligned systems by solid-state NMR magic angle spinning methods.. https://doi.org/10.1016/j.jmr.2005.06.008

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