Evidence map›Paper›PMID 31041648›Full record

ArticleJournal of biomolecular NMR2019

Super resolution NOESY spectra of proteins.

Charles F DeLisle, H Bhagya Mendis, Justin L Lorieau

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Homonuclear Super-Resolution NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2024
    Article
  2. 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

3 authors.

Charles F DeLisleDepartment of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL, 60607, USA.
H Bhagya MendisDepartment of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL, 60607, USA.
Justin L LorieauDepartment of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL, 60607, USA. justin@lorieau.com.ORCID http://orcid.org/0000-0001-6257-5561

Funding

National Science Foundation 1651598
6 · The paper itself

Abstract

Spectral resolution remains one of the most significant limitations in the NMR study of biomolecules. We present the srNOESY (super resolution nuclear overhauser effect spectroscopy) experiment, which enhances the resolution of NOESY cross-peaks at the expense of the diagonal peak line-width. We studied two proteins, ubiquitin and the influenza hemagglutinin fusion peptide in bicelles, and we achieved average resolution enhancements of 21-47% and individual peak enhancements as large as ca. 450%. New peaks were observed over the conventional NOESY experiment in both proteins as a result of these improvements, and the final structures generated from the calculated restraints matched published models. We discuss the impact of the experimental parameters, spin diffusion and the information content of the srNOESY lineshape.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAlgorithmsMagnetic Resonance SpectroscopyModels, MolecularModels, TheoreticalProteinsProteinsNOESYProteinsResolution enhancementSignal improvementSolution-state NMRSRNOESY

Identifiers

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.