Evidence map›Paper›PMID 33087707›Full record

ArticleNature communications2020

Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids.

Mihajlo Novakovic, Ēriks Kupče, Andreas Oxenfarth, Marcos D Battistel, Darón I Freedberg, Harald Schwalbe, Lucio Frydman

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  6. Identifying and Overcoming Artifacts inJournal of the American Chemical Society · 2023
    Article
  7. Review
  8. The Extended Hadamard Transform: Sensitivity-Enhanced NMR Experiments Among Labile and Non-LabileChemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  9. Structural Elucidation and Activities ofFrontiers in nutrition · 2022
    Review
  10. Article
  11. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.Angewandte Chemie (International ed. in English) · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

Mihajlo NovakovicDepartment of Chemical and Biological Physics, Weizmann Institute of Science, 7610001, Rehovot, Israel.
Ēriks KupčeBruker UK Ltd., Banner Lane, Coventry, UK.
Andreas OxenfarthInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University, D-60438, Frankfurt/Main, Germany.
Marcos D BattistelLaboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Food and Drug Administration, 10903 New Hampshire Ave, Silver Spring, MD, 20993, USA.
Darón I FreedbergLaboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Food and Drug Administration, 10903 New Hampshire Ave, Silver Spring, MD, 20993, USA.ORCID 0000-0003-1991-5174
Harald SchwalbeInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University, D-60438, Frankfurt/Main, Germany.
Lucio FrydmanDepartment of Chemical and Biological Physics, Weizmann Institute of Science, 7610001, Rehovot, Israel. lucio.frydman@weizmann.ac.il.ORCID 0000-0001-8208-3521
Center for Biologics Evaluation and Research · USGoethe University Frankfurt · DEWeizmann Institute of Science · ILCoventry (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multidimensional TOCSY and NOESY are central experiments in chemical and biophysical NMR. Limited efficiencies are an intrinsic downside of these methods, particularly when targeting labile sites. This study demonstrates that the decoherence imparted on these protons through solvent exchanges can, when suitably manipulated, lead to dramatic sensitivity gains per unit time in the acquisition of these experiments. To achieve this, a priori selected frequencies are encoded according to Hadamard recipes, while concurrently subject to looped selective inversion or selective saturation procedures. Suitable processing then leads to protein, oligosaccharide and nucleic acid cross-peak enhancements of ≈200-1000% per scan, in measurements that are ≈10-fold faster than conventional counterparts. The extent of these gains will depend on the solvent exchange and relaxation rates of the targeted sites; these gains also benefit considerably from the spectral resolution provided by ultrahigh fields, as corroborated by NMR experiments at 600 MHz and 1 GHz. The mechanisms underlying these experiments' enhanced efficiencies are analyzed on the basis of three-way polarization transfer interplays between the water, labile and non-labile protons, and the experimental results are rationalized using both analytical and numerical derivations. Limitations as well as further extensions of the proposed methods, are also discussed.

Indexed as

Binding SitesMagnetic Resonance SpectroscopyMolecular StructureNuclear Magnetic Resonance, BiomolecularNucleic AcidsPolysaccharidesProteinsNucleic AcidsPolysaccharidesProteins

Identifiers

PMID33087707
PMCPMC7577996
OpenAlexW3023241931

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.