TY - JOUR AB - 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. AU - Kurauskas, Vilius AU - Crublet, Elodie AU - Macek, Pavel AU - Kerfah, Rime AU - Gauto, Diego F. AU - Boisbouvier, Jérôme AU - Schanda, Paul ID - 8455 IS - 61 JF - Chemical Communications KW - Materials Chemistry KW - Electronic KW - Optical and Magnetic Materials KW - General Chemistry KW - Surfaces KW - Coatings and Films KW - Metals and Alloys KW - Ceramics and Composites KW - Catalysis SN - 1359-7345 TI - Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit VL - 52 ER -