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Updated: Mar 18, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to
Vilius Kurauskas1, Elodie Crublet1, Pavel Macek1
1Université Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France. crublet@nmr-bio.com schanda@ibs.fr and CEA, Institut de Biologie Structurale, F-38044 Grenoble, France and CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
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.
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