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High resolution H-detected solid-state NMR spectroscopy of protein aliphatic resonances: Access to tertiary structure information

Journal of the American Chemical Society, ISSN: 0002-7863, Vol: 132, Issue: 43, Page: 15133-15135
2010
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Article Description

Biological magic angle spinning (MAS) solid-state nuclear magnetic resonance spectroscopy has developed rapidly over the past two decades. For the structure determination of a protein by solid-state NMR, routinely C,C distance restraints as well as dihedral restraints are employed. In protonated samples, this is achieved by growing the bacterium on a medium which contains [1,3]-C glycerol or [2]-C glycerol to dilute the C spin system. Labeling schemes, which rely on heteronuclei, are insensitive both for detection and in terms of quantification of distances, since they are relying on low-γ nuclei. Proton detection can in principle provide a gain in sensitivity by a factor of 8 and 31, compared to the C or N detected version of the experiment. We report here a new labeling scheme, which enables H-detection of aliphatic resonances with high resolution in MAS solid-state NMR spectroscopy. We prepared microcrystals of the SH3 domain of chicken α-spectrin with 5% protonation at nonexchangeable sites and obtained line widths on the order of 25 Hz for aliphatic H resonances. We show further that C resolved 3D-H, H correlation experiments yield access to long-range proton-proton distances in the protein. © 2010 American Chemical Society.

Bibliographic Details

Asami, Sam; Schmieder, Peter; Reif, Bernd

American Chemical Society (ACS)

Chemical Engineering; Chemistry; Biochemistry, Genetics and Molecular Biology

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