ArticleJournal of biomolecular NMR2009
Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 125 citations in OpenAlex.
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- Solid-state NMR protocols for unveiling dynamics and (drug) interactions of membrane-bound proteins.Protein science : a publication of the Protein Society · 2025Article
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- Atomic structure of the open SARS-CoV-2 E viroporin.Science advances · 2023Article
- Atomic-Resolution Structure of the Protein Encoded by Gene V of fd Bacteriophage in Complex with Viral ssDNA Determined by Magic-Angle Spinning Solid-State NMR.Journal of the American Chemical Society · 2023Article
- Protein resonance assignment by solid-state NMR based onJournal of biomolecular NMR · 2021Article
- Extensively sparseJournal of biomolecular NMR · 2021Article
- RIP2 filament formation is required for NOD2 dependent NF-κB signalling.Nature communications · 2018Article
- Segmental isotope labelling and solid-state NMR of a 12 × 59 kDa motor protein: identification of structural variability.Journal of biomolecular NMR · 2018Article
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Direct assignment ofJournal of biomolecular NMR · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Structure of outer membrane protein G in lipid bilayers.Nature communications · 2017Article
- Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.Journal of biomolecular NMR · 2017Article
- Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Journal of visualized experiments : JoVE · 2017Article
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
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- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, solid-state magic-angle spinning nuclear magnetic resonance spectroscopy (MAS NMR) has been growing into an important technique to study the structure of membrane proteins, amyloid fibrils and other protein preparations which do not form crystals or are insoluble. Currently, a key bottleneck is the assignment process due to the absence of the resolving power of proton chemical shifts. Particularly for large proteins (approximately >150 residues) it is difficult to obtain a full set of resonance assignments. In order to address this problem, we present an assignment method based upon samples prepared using [1,3-13C]- and [2-13C]-glycerol as the sole carbon source in the bacterial growth medium (so-called selectively and extensively labelled protein). Such samples give rise to higher quality spectra than uniformly [13C]-labelled protein samples, and have previously been used to obtain long-range restraints for use in structure calculations. Our method exploits the characteristic cross-peak patterns observed for the different amino acid types in 13C-13C correlation and 3D NCACX and NCOCX spectra. An in-depth analysis of the patterns and how they can be used to aid assignment is presented, using spectra of the chicken alpha-spectrin SH3 domain (62 residues), alphaB-crystallin (175 residues) and outer membrane protein G (OmpG, 281 residues) as examples. Using this procedure, over 90% of the Calpha, Cbeta, C' and N resonances in the core domain of alphaB-crystallin and around 73% in the flanking domains could be assigned (excluding 24 residues at the extreme termini of the protein).
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