Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit

Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda P. 2016. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 52(61), 9558–9561.

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Journal Article | Published | English
Author
Kurauskas, Vilius; Crublet, Elodie; Macek, Pavel; Kerfah, Rime; Gauto, Diego F.; Boisbouvier, Jérôme; Schanda, PaulISTA
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.
Publishing Year
Date Published
2016-07-04
Journal Title
Chemical Communications
Volume
52
Issue
61
Page
9558-9561
IST-REx-ID

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Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 2016;52(61):9558-9561. doi:10.1039/c6cc04484k
Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., & Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. Royal Society of Chemistry. https://doi.org/10.1039/c6cc04484k
Kurauskas, Vilius, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F. Gauto, Jérôme Boisbouvier, and Paul Schanda. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome Subunit.” Chemical Communications. Royal Society of Chemistry, 2016. https://doi.org/10.1039/c6cc04484k.
V. Kurauskas et al., “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit,” Chemical Communications, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.
Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda P. 2016. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 52(61), 9558–9561.
Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome Subunit.” Chemical Communications, vol. 52, no. 61, Royal Society of Chemistry, 2016, pp. 9558–61, doi:10.1039/c6cc04484k.

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