Evidence map›Paper›PMID 26267840›Full record

ArticleJournal of biomolecular NMR2015

Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods.

Susanne Penzel, Albert A Smith, Vipin Agarwal, Andreas Hunkeler, Mai-Liis Org, Ago Samoson, Anja Böckmann, Matthias Ernst, Beat H Meier

Abstract read
PubMed Publisher
In one paragraph

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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.The journal of physical chemistry letters · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Characterization of peptide O⋯HN hydrogen bondsChemical communications (Cambridge, England) · 2023
    Article
  9. Review
  10. Article
  11. Solid state nuclear magnetic resonance · 2022
    Article
  12. Article
  13. Residue-Specific High-ResolutionThe journal of physical chemistry letters · 2022
    Article
  14. Review
  15. Chemical reviews · 2022
    Review
  16. Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensionalProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. A pocket-factor-triggered conformational switch in the hepatitis B virus capsid.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Article
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

9 authors.

Susanne PenzelPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
Albert A SmithPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
Vipin AgarwalPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
Andreas HunkelerPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
Mai-Liis OrgNMR Instituut, Tartu Teadus, Tehnomeedikum, Tallinn University of Technology, Akadeemia tee 15a, 19086, Tallinn, Estonia.
Ago SamosonNMR Instituut, Tartu Teadus, Tehnomeedikum, Tallinn University of Technology, Akadeemia tee 15a, 19086, Tallinn, Estonia. ago.samoson@ttu.ee.
Anja BöckmannInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7, passage du Vercors, 69367, Lyon, France. a.bockmann@ibcp.fr.
Matthias ErnstPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland. maer@ethz.ch.
Beat H MeierPhysical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland. beme@ethz.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100 kHz. We present a systematic examination of the MAS dependence of the amide proton T 2' times and a site-specific comparison of T 2' at 93 kHz versus 60 kHz MAS frequency. A quantitative analysis of transfer efficiencies of building blocks, as they are used for typical 3D experiments, was performed. To do this, we compared dipolar-coupling and J-coupling based transfer steps. The building blocks were then combined into 3D experiments for sequential resonance assignment, where we evaluated signal-to-noise ratio and information content of the different 3D spectra in order to identify the best assignment strategy. Based on this comparison, six experiments were selected to optimally assign the model protein ubiquitin, solely using spectra acquired at 93 kHz MAS. Within 3 days of instrument time, the required spectra were recorded from which the backbone resonances have been assigned to over 96%.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProteinsProteinsAssignmentMASSolid-state NMR

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.