Evidence map›Paper›PMID 29502224›Full record

ArticleJournal of biomolecular NMR2018

Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR.

James Tolchard, Manoj Kumar Pandey, Mélanie Berbon, Abdelmajid Noubhani, Sven J Saupe, Yusuke Nishiyama, Birgit Habenstein, Antoine Loquet

Abstract read
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Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Design Parameters of Tissue-Engineering Scaffolds at the Atomic Scale.Angewandte Chemie (International ed. in English) · 2019
    Article
  6. Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    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

8 authors.

James TolchardInstitute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600, Pessac, France.
Manoj Kumar PandeyJEOL RESONANCE Inc., Musashino, Akishima, Tokyo, 196-8558, Japan.
Mélanie BerbonInstitute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600, Pessac, France.
Abdelmajid NoubhaniInstitute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600, Pessac, France.
Sven J SaupeInstitut de Biochimie et de Génétique Cellulaire, (UMR 5095 IBGC), CNRS, Université Bordeaux, 33077, Bordeaux, France.
Yusuke NishiyamaJEOL RESONANCE Inc., Musashino, Akishima, Tokyo, 196-8558, Japan. yunishiy@jeol.co.jp.
Birgit HabensteinInstitute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600, Pessac, France. b.habenstein@iecb.u-bordeaux.fr.
Antoine LoquetInstitute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600, Pessac, France. a.loquet@iecb.u-bordeaux.fr.ORCID 0000-0001-7176-7813

Funding

Agence Nationale de la Recherche ANR-13-PDOC-0017-01Agence Nationale de la Recherche ANR-17-CE11-0035Agence Nationale de la Recherche (FR) ANR-14-CE09-0020-01Centre National de la Recherche Scientifique IR-RMN FR3050European Research Council 639020IdEx Bordeaux ANR-10-IDEX-03-02
6 · The paper itself

Abstract

We present a new solid-state NMR proton-detected three-dimensional experiment dedicated to the observation of protein proton side chain resonances in nano-liter volumes. The experiment takes advantage of very fast magic angle spinning and double quantum 13C-13C transfer to establish efficient (H)CCH correlations detected on side chain protons. Our approach is demonstrated on the HET-s prion domain in its functional amyloid fibrillar form, fully protonated, with a sample amount of less than 500 µg using a MAS frequency of 70 kHz. The majority of aliphatic and aromatic side chain protons (70%) are observable, in addition to Hα resonances, in a single experiment providing a complementary approach to the established proton-detected amide-based multidimensional solid-state NMR experiments for the study and resonance assignment of biosolid samples, in particular for aromatic side chain resonances.

Indexed as

ProtonsAmyloidCarbon IsotopesNuclear Magnetic Resonance, BiomolecularPrionsAmyloidCarbon-13Carbon IsotopesPrionsProtonsAmyloid fibrilsProtein NMRProton detectionSolid-state NMRVery fast MAS

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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.