ArticleJournal of biomolecular NMR2015
Real-time pure shift ¹⁵N HSQC of proteins: a real improvement in resolution and sensitivity.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Dual bilinear rotations.Magnetic resonance (Gottingen, Germany) · 2026Article
- Robust bilinear rotations II.Magnetic resonance (Gottingen, Germany) · 2026Article
- Robust bilinear rotations.Science advances · 2025Article
- Pure shift amide detection in conventional and TROSY-type experiments ofJournal of biomolecular NMR · 2022Article
- NMR Spectroscopy for Metabolomics Research.Metabolites · 2019Review
- Real-Time Pure Shift HSQC NMR for Untargeted Metabolomics.Analytical chemistry · 2019Article
- Practical aspects of real-time pure shift HSQC experiments.Magnetic resonance in chemistry : MRC · 2018Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
Abstract
Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here. Both resolution and sensitivity are improved, without any increase in experiment time. In these experiments, free induction decays are collected in short bursts of data acquisition, with durations short on the timescale of J-evolution, interspersed with suitable refocusing elements. The net effect is real-time (t 2) broadband homodecoupling, suppressing the multiplet structure caused by proton-proton interactions. The key feature of the refocusing elements is that they discriminate between the resonances of active (observed) and passive (coupling partner) spins. This can be achieved either by using band-selective refocusing or by the BIRD element, in both cases accompanied by a nonselective 180° proton pulse. The latter method selects the active spins based on their one-bond heteronuclear J-coupling to (15)N, while the former selects a region of the (1)H spectrum. Several novel pure shift experiments are presented, and the improvements in resolution and sensitivity they provide are evaluated for representative samples: the N-terminal domain of PGK; ubiquitin; and two mutants of the small antifungal protein PAF. These new experiments, delivering improved sensitivity and resolution, have the potential to replace the current standard HSQC experiments.
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Registered trials
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