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Xue, K. ; Sarkar, R. ; Motz, C.* ; Asami, S.* ; Camargo, D.C.R.* ; Decker, V.* ; Wegner, S.* ; Tosner, Z.* ; Reif, B.

Limits of resolution and sensitivity of proton detected MAS solid-state NMR experiments at 111 kHz in deuterated and protonated proteins.

Sci. Rep. 7:7444 (2017)

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MAS solid-state NMR is capable of determining structures of protonated solid proteins using proton-detected experiments. These experiments are performed at MAS rotation frequency of around 110 kHz, employing 0.5 mg of material. Here, we compare (1)H, (13)C correlation spectra obtained from protonated and deuterated microcrystalline proteins at MAS rotation frequency of 111 kHz, and show that the spectral quality obtained from deuterated samples is superior to those acquired using protonated samples in terms of resolution and sensitivity. In comparison to protonated samples, spectra obtained from deuterated samples yield a gain in resolution on the order of 3 and 2 in the proton and carbon dimensions, respectively. Additionally, the spectrum from the deuterated sample yields approximately 2-3 times more sensitivity compared to the spectrum of a protonated sample. This gain could be further increased by a factor of 2 by making use of stereospecific precursors for biosynthesis. Although the overall resolution and sensitivity of (1)H, (13)C correlation spectra obtained using protonated solid samples with rotation frequencies on the order of 110 kHz is high, the spectral quality is still poor when compared to the deuterated samples. We believe that experiments involving large protein complexes in which sensitivity is limiting will benefit from the application of deuteration schemes.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Angle-spinning Nmr; Perdeuterated Proteins; Resonance Assignment; Amyloid Fibrils; Aliphatic Sites; Methyl-groups; Spectroscopy; Strategies; Dynamics; Subunit

ISSN (print) / ISBN 2045-2322

e-ISSN 2045-2322

Journal Scientific Reports

Quellenangaben Volume: 7, Issue: 1, Article Number: 7444

Publisher Nature Publishing Group

Publishing Place London

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)