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Issue 61, 2016
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Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit

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Abstract

Solid-state NMR spectroscopy allows the characterization of the structure, interactions and dynamics of insoluble and/or very large proteins. Sensitivity and resolution are often major challenges for obtaining atomic-resolution information, in particular for very large protein complexes. Here we show that the use of deuterated, specifically CH3-labelled proteins result in significant sensitivity gains compared to previously employed CHD2 labelling, while line widths increase only marginally. We apply this labelling strategy to a 468 kDa-large dodecameric aminopeptidase, TET2, and the 1.6 MDa-large 50S ribosome subunit of Thermus thermophilus.

Graphical abstract: Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit

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Publication details

The article was received on 31 May 2016, accepted on 04 Jul 2016 and first published on 04 Jul 2016


Article type: Communication
DOI: 10.1039/C6CC04484K
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Citation: Chem. Commun., 2016,52, 9558-9561
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    Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit

    V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D. F. Gauto, J. Boisbouvier and P. Schanda, Chem. Commun., 2016, 52, 9558
    DOI: 10.1039/C6CC04484K

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