Evidence map›Paper›PMID 25102442›Full record

ArticleJournal of the American Chemical Society2014

Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.

Emeline Barbet-Massin, Andrew J Pell, Joren S Retel, Loren B Andreas, Kristaps Jaudzems, W Trent Franks, Andrew J Nieuwkoop, Matthias Hiller, Victoria Higman, Paul Guerry and 18 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing 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

157 citing papers in PubMed.

  1. Article
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  4. Review
  5. Super-Resolution solid-state NMR Spectroscopy.Journal of biomolecular NMR · 2026
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  9. The Structure of Human IAPP Fibrils Reflects Membrane and pH Conditions.Journal of the American Chemical Society · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Conformational Analysis of UniformlyMolecules (Basel, Switzerland) · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Analysis of the structure and interactions of the SARS-CoV-2 ORF7b accessory protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article

97 more citing papers are in PubMed but not listed here.

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

28 authors.

Emeline Barbet-MassinCentre de RMN à Très Hauts Champs, Institut des Sciences Analytiques (CNRS, ENS Lyon, UCB Lyon 1), Université de Lyon , 69100 Villeurbanne, France.
Andrew J Pell
Joren S Retel
Loren B Andreas
Kristaps Jaudzems
W Trent Franks
Andrew J Nieuwkoop
Matthias Hiller
Victoria Higman
Paul Guerry
Andrea Bertarello
Michael J Knight
Michele Felletti
Tanguy Le Marchand
Svetlana Kotelovica
Inara Akopjana
Kaspars Tars
Monica Stoppini
Vittorio Bellotti
Martino Bolognesi
Stefano Ricagno
James J Chou
Robert G Griffin
Hartmut Oschkinat
Anne Lesage
Lyndon Emsley
Torsten Herrmann
Guido Pintacuda

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Solid State NMR Studies of Membrane ProteinsR01EB001960 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2017
$6.5M
Medical Research Council MR/K000187/1NIBIB NIH HHS EB-001960NIBIB NIH HHS EB-002026NIBIB NIH HHS P41 EB002026
6 · The paper itself

Abstract

Using a set of six (1)H-detected triple-resonance NMR experiments, we establish a method for sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectra of 5-30 kDa proteins. The approach relies on perdeuteration, amide (2)H/(1)H exchange, high magnetic fields, and high-spinning frequencies (ωr/2π ≥ 60 kHz) and yields high-quality NMR data, enabling the use of automated analysis. The method is validated with five examples of proteins in different condensed states, including two microcrystalline proteins, a sedimented virus capsid, and two membrane-embedded systems. In comparison to contemporary (13)C/(15)N-based methods, this approach facilitates and accelerates the MAS NMR assignment process, shortening the spectral acquisition times and enabling the use of unsupervised state-of-the-art computational data analysis protocols originally developed for solution NMR.

Indexed as

ProtonsCarbon IsotopesDeuterium Exchange MeasurementHydrogenModels, MolecularNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProteinsCarbon IsotopesHydrogenNitrogen IsotopesProteinsProtons

Identifiers

PMID25102442
PMCPMC4156866

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.