Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Chemical Communications Année : 2016

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

Résumé

Solid-state NMR spectroscopy allows the characterization of 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 only marginally increase. 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.
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Dates et versions

hal-01353309 , version 1 (11-08-2016)

Identifiants

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Vilius Kurauskas, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego Gauto, et al.. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit. Chemical Communications, 2016, 52, pp.9558-9561. ⟨10.1039/C6CC04484K⟩. ⟨hal-01353309⟩
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