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A solid-state 17O NMR 1H-decoupled double angle rotation (DOR) study of monosodium l-glutamate monohydrate (l-MSG) is reported. It is shown that all eight inequivalent sites can be resolved with DOR line widths ( approximately 65 Hz) approximately 120 times narrower than those in the MAS spectrum. The lines are tentatively assigned on the basis of their behavior under proton decoupling and the isotropic chemical shift and the quadrupole interaction parameter for each extracted by a combination of DOR and 3Q MAS at variable magnetic fields. With a shift range of approximately 45 ppm for these similar oxygen sites and spectral resolution under DOR comparable to that for spin-1/2 nuclei, solid-state 17O NMR should have tremendous potential in the study of biomolecules.

Original publication

DOI

10.1021/ja062031l

Type

Journal article

Journal

J Am Chem Soc

Publication Date

21/06/2006

Volume

128

Pages

7744 - 7745

Keywords

Binding Sites, Deuterium, Nuclear Magnetic Resonance, Biomolecular, Oxygen, Oxygen Isotopes, Proteins