Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 9, Pages 2438-2442Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201308927
Keywords
deuteration; high sensitivity; proteins; quadruple-resonance MAS NMR spectroscopy; structure elucidation
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Funding
- European Union [2618633]
- Deutsche Forschungsgemeinschaft [05106/12-1]
- Danish National Research Foundation [DNRF59]
- Alexander von Humboldt Foundation
- Fulbright Commission
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H-1-detected magic-angle spinning NMR experiments facilitate structural biology of solid proteins, which requires using deuterated proteins. However, often amide protons cannot be back-exchanged sufficiently, because of a possible lack of solvent exposure. For such systems, using H-2 excitation instead of H-1 excitation can be beneficial because of the larger abundance and shorter longitudinal relaxation time, T-1, of deuterium. A new structure determination approach, quadruple-resonance NMR spectroscopy, is presented which relies on an efficient H-2-excitation and H-2-C-13 cross-polarization (CP) step, combined with H-1 detection. We show that by using H-2-excited experiments better sensitivity is possible on an SH3 sample recrystallized from 30% H2O. For a membrane protein, the ABC transporter ArtMP in native lipid bilayers, different sets of signals can be observed from different initial polarization pathways, which can be evaluated further to extract structural properties.
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