ArticleJournal of biomolecular NMR2016
Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids.
Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026Article
- Protein-tags and their fragments as potent inhibitors of enzymes: Structure of the ternary complex of phosphopantetheine adenylyltransferase from Enterobacter spp. with tag-peptides and phosphonoacetic acid at 2.20 Å resolution.Protein science : a publication of the Protein Society · 2025Article
- Structure of a novel form of phosphopantetheine adenylyltransferase from Klebsiella pneumoniae at 2.59 Å resolution.European biophysics journal : EBJ · 2024Article
- Methyl probes in proteins for determining ligand binding mode in weak protein-ligand complexes.Scientific reports · 2022Article
- Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins.Journal of biomolecular NMR · 2022Article
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Protein-ligand structure determination with the NMR molecular replacement tool, NMRJournal of biomolecular NMR · 2020Article
- NMR spectroscopy: the swiss army knife of drug discovery.Journal of biomolecular NMR · 2020Article
- Article
- Automatic structure-based NMR methyl resonance assignment in large proteins.Nature communications · 2019Article
- Characterizing Protein Hydration Dynamics Using Solution NMR Spectroscopy.Methods in enzymology · 2019Article
- Assigning methyl resonances for protein solution-state NMR studies.Methods (San Diego, Calif.) · 2018Article
- Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules.Journal of biomolecular NMR · 2018Article
- Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methyl-methyl NOESY.Journal of biomolecular NMR · 2018Article
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Authors and funding
5 authors.
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Abstract
The deuteration of proteins and selective labeling of side chain methyl groups has greatly enhanced the molecular weight range of proteins and protein complexes which can be studied using solution NMR spectroscopy. Protocols for the selective labeling of all six methyl group containing amino acids individually are available, however to date, only a maximum of five amino acids have been labeled simultaneously. Here, we describe a new methodology for the simultaneous, selective labeling of all six methyl containing amino acids using the 115 kDa homohexameric enzyme CoaD from E. coli as a model system. The utility of the labeling protocol is demonstrated by efficiently and unambiguously assigning all methyl groups in the enzymatic active site using a single 4D (13)C-resolved HMQC-NOESY-HMQC experiment, in conjunction with a crystal structure. Furthermore, the six fold labeled protein was employed to characterize the interaction between the substrate analogue (R)-pantetheine and CoaD by chemical shift perturbations, demonstrating the benefit of the increased probe density.
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