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Xue, K. ; Sarkar, R. ; Tosner, Z.* ; Lalli, D.* ; Motz, C.* ; Koch, B.* ; Pintacuda, G.* ; Reif, B.

MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR.

J. Biomol. NMR 73, 625-631 (2019)

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Sensitivity and resolution together determine the quality of NMR spectra in biological solids. For high-resolution structure determination with solid-state NMR, proton-detection emerged as an attractive strategy in the last few years. Recent progress in probe technology has extended the range of available MAS frequencies up to above 100 kHz, enabling the detection of resolved resonances from sidechain protons, which are important reporters of structure. Here we characterise the interplay between MAS frequency in the newly available range of 70-110 kHz and proton content on the spectral quality obtainable on a 1 GHz spectrometer for methyl resonances. Variable degrees of proton densities are tested on microcrystalline samples of the alpha-spectrin SH3 domain with selectively protonated methyl isotopomers (CH3, CH2D, CHD2) in a perdeuterated matrix. The experimental results are supported by simulations that allow the prediction of the sensitivity outside this experimental frequency window. Our results facilitate the selection of the appropriate labelling scheme at a given MAS rotation frequency.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Solid State Nmr ; Magic Angle Spinning (mas) ; Selective Deuteration ; Ch3 Labelling ; Methyl Isotopomers ; Microcrystalline Proteins; High-resolution; 100 Khz; Perdeuterated Proteins; Resonance Assignment; Spectroscopy; Spectra; Enhancement

ISSN (print) / ISBN 0925-2738

e-ISSN 1573-5001

Journal Journal of Biomolecular NMR

Quellenangaben Volume: 73, Issue: 10-11, Pages: 625-631

Publisher Springer

Publishing Place Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)