ArticleJournal of biomolecular NMR2014
A 3D time-shared NOESY experiment designed to provide optimal resolution for accurate assignment of NMR distance restraints in large 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 7 papers.
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Who cites it
7 citing papers in PubMed.
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.Nucleic acids research · 2025Article
- Global protein dynamics as communication sensors in peptide synthetase domains.Science advances · 2022Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- The 3-D conformational shape of N-naphthyl-cyclopenta[d]pyrimidines affects their potency as microtubule targeting agents and their antitumor activity.Bioorganic & medicinal chemistry · 2021Article
- NMR: an essential structural tool for integrative studies of T cell development, pMHC ligand recognition and TCR mechanobiology.Journal of biomolecular NMR · 2019Article
- Effortless assignment with 4D covariance sequential correlation maps.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps.Journal of biomolecular NMR · 2015Article
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3 authors.
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Abstract
Structure determination of proteins by solution NMR has become an established method, but challenges increase steeply with the size of proteins. Notably, spectral crowding and signal overlap impair the analysis of cross-peaks in NOESY spectra that provide distance restraints for structural models. An optimal spectral resolution can alleviate overlap but requires prohibitively long experimental time with existing methods. Here we present a time-shared 3D experiment optimized for large proteins that provides ¹⁵N and ¹³C dispersed NOESY spectra in a single measurement. NOESY correlations appear in the detected dimension and hence benefit from the highest resolution achievable of all dimensions without increase in experimental time. By design, this experiment is inherently optimal for non-uniform sampling acquisition when compared to current alternatives. Thus, ¹⁵N and ¹³C dispersed NOESY spectra with ultra-high resolution in all dimensions were acquired in parallel within about 4 days instead of 80 days for a 52 kDa monomeric protein at a concentration of 350 μM.
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