ArticleJournal of biomolecular NMR2014
Improved NMR experiments with ¹³C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
Article in Journal of biomolecular NMR, 2014. 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.
- The perfect carbon TOCSY (iPE TOCSY) facilitates assignment of large biomolecules.Journal of biomolecular NMR · 2026Article
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.Nucleic acids research · 2025Article
- Isoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR.Journal of the American Chemical Society · 2025Article
- Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6.Structure (London, England : 1993) · 2024Article
- The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation.Nature communications · 2022Article
- Efficient affinity ranking of fluorinated ligands byJournal of biomolecular NMR · 2020Article
- Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase.Biomolecules · 2019Article
- Overcoming Drug Resistance through the Development of Selective Inhibitors of UDP-Glucuronosyltransferase Enzymes.Journal of molecular biology · 2019Article
- Inhibition of prenylated KRAS in a lipid environment.PloS one · 2017Article
- Analytical optimization of active bandwidth and quality factor for TOCSY experiments in NMR spectroscopy.Journal of biomolecular NMR · 2016Article
- A new broadband homonuclear mixing pulse for NMR with low applied power.The Journal of chemical physics · 2014Article
- Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy.The Journal of biological chemistryArticle
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Abstract
Three improved ¹³C-spinlock experiments for side chain assignments of isotope labelled proteins in liquid state are presented. These are based on wide bandwidth spinlock techniques that have become possible with contemporary cryogenic probes. The first application, the H(C(ali)C(aro))H-TOCSY, is an HCCH-TOCSY in which all CHn moieties of a protein are detected in a single experiment, including the aromatic ones. This enables unambiguous assignment of aromatic and aliphatic amino acids in a single, highly sensitive experiment. In the second application, the ¹³C-detected C(all)-TOCSY, magnetization transfer comprises all carbons--aliphatic, aromatic as well as the carbonyl carbons--making the complete carbon assignment possible using one spectrum only. Thirdly, the frequently used HC(CCO)NH experiment was redesigned by replacing the long C-carbonyl refocused INEPT transfer step by direct ¹³C-¹³C-TOCSY magnetization transfer from side chain carbons to the backbone carbonyls. The resulting HC(CCO)NH experiment minimizes relaxation losses because it is shorter and represents a more sensitive alternative particularly for larger proteins. The performance of the experiments is demonstrated on isotope labeled proteins up to the size of 43 kDa.
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