ArticleJournal of biomolecular NMR2013
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 30 citations in OpenAlex.
- Conformation-selective detection of residues in solid proteins under magic-angle-spinning.Journal of biomolecular NMR · 2026Article
- Super-resolution triple-resonance NMR spectroscopy for the sequential assignment of proteins.Science advances · 2025Article
- Analysis of the homodimeric structure of a D-Ala-D-Ala metallopeptidase, VanX, from vancomycin-resistant bacteria.Protein science : a publication of the Protein Society · 2024Article
- Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation.Biochemical Society transactions · 2022Review
- NMR resonance assignments of human Atg3 in aqueous solution and bicelles.Biomolecular NMR assignments · 2021Article
- Allosteric Impact of the Variable Insert Loop inBiochemistry · 2020Article
- De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Opportunities and Challenges of Backbone, Sidechain, and RDC Experiments to Study Membrane Protein Dynamics in a Detergent-Free Lipid Environment Using Solution State NMR.Frontiers in molecular biosciences · 2019Review
- Mechanism of APTX nicked DNA sensing and pleiotropic inactivation in neurodegenerative disease.The EMBO journal · 2018Article
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.Nature structural & molecular biology · 2017Article
- The ABC exporter MsbA probed by solid state NMR – challenges and opportunities.Biological chemistry · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
NMR-based structure determination of a protein requires the assignment of resonances as indispensable first step. Even though heteronuclear through-bond correlation methods are available for that purpose, challenging situations arise in cases where the protein in question only yields samples of limited concentration and/or stability. Here we present a strategy based upon specific individual unlabeling of all 20 standard amino acids to complement standard NMR experiments and to achieve unambiguous backbone assignments for the fast precipitating 23 kDa catalytic domain of human aprataxin of which only incomplete standard NMR data sets could be obtained. Together with the validation of this approach utilizing the protein GB1 as a model, a comprehensive insight into metabolic interconversion ("scrambling") of NH and CO groups in a standard Escherichia coli expression host is provided.
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