{"language":[{"iso":"eng"}],"keyword":["Materials Chemistry","Electronic","Optical and Magnetic Materials","General Chemistry","Surfaces","Coatings and Films","Metals and Alloys","Ceramics and Composites","Catalysis"],"article_processing_charge":"No","publication_status":"published","publication_identifier":{"issn":["1359-7345","1364-548X"]},"citation":{"ieee":"V. Kurauskas <i>et al.</i>, “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit,” <i>Chemical Communications</i>, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.","ista":"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.","ama":"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. <i>Chemical Communications</i>. 2016;52(61):9558-9561. doi:<a href=\"https://doi.org/10.1039/c6cc04484k\">10.1039/c6cc04484k</a>","chicago":"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.” <i>Chemical Communications</i>. Royal Society of Chemistry, 2016. <a href=\"https://doi.org/10.1039/c6cc04484k\">https://doi.org/10.1039/c6cc04484k</a>.","short":"V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier, P. Schanda, Chemical Communications 52 (2016) 9558–9561.","apa":"Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., &#38; Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. <i>Chemical Communications</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c6cc04484k\">https://doi.org/10.1039/c6cc04484k</a>","mla":"Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome Subunit.” <i>Chemical Communications</i>, vol. 52, no. 61, Royal Society of Chemistry, 2016, pp. 9558–61, doi:<a href=\"https://doi.org/10.1039/c6cc04484k\">10.1039/c6cc04484k</a>."},"author":[{"full_name":"Kurauskas, Vilius","last_name":"Kurauskas","first_name":"Vilius"},{"full_name":"Crublet, Elodie","last_name":"Crublet","first_name":"Elodie"},{"full_name":"Macek, Pavel","last_name":"Macek","first_name":"Pavel"},{"last_name":"Kerfah","first_name":"Rime","full_name":"Kerfah, Rime"},{"full_name":"Gauto, Diego F.","last_name":"Gauto","first_name":"Diego F."},{"last_name":"Boisbouvier","first_name":"Jérôme","full_name":"Boisbouvier, Jérôme"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"issue":"61","date_published":"2016-07-04T00:00:00Z","type":"journal_article","month":"07","year":"2016","status":"public","intvolume":"        52","publisher":"Royal Society of Chemistry","doi":"10.1039/c6cc04484k","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"04","quality_controlled":"1","volume":52,"date_updated":"2021-01-12T08:19:23Z","abstract":[{"text":"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.","lang":"eng"}],"publication":"Chemical Communications","date_created":"2020-09-18T10:07:29Z","page":"9558-9561","_id":"8455","oa_version":"None","title":"Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit","article_type":"original"}