Evidence map›Paper›PMID 26494649›Full record

ArticleJournal of biomolecular NMR2015

Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.

Meaghan E Ward, Emily Ritz, Mumdooh A M Ahmed, Vladimir V Bamm, George Harauz, Leonid S Brown, Vladimir Ladizhansky

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  3. Review
  4. Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020
    Review
  5. Article
  6. Alpha protons as NMR probes in deuterated proteins.Journal of biomolecular NMR · 2019
    Article
  7. Review
  8. Site-Specific Studies of Nucleosome Interactions by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2018
    Article
  9. Article
  10. Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017
    Article
  11. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  12. 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

7 authors at 1 institution in 1 country.

Meaghan E WardDepartment of Physics, University of Guelph, Guelph, ON, Canada.
Emily RitzDepartment of Physics, University of Guelph, Guelph, ON, Canada.
Mumdooh A M AhmedDepartment of Physics, University of Guelph, Guelph, ON, Canada.
Vladimir V BammBiophysics Interdepartmental Group, University of Guelph, Guelph, ON, Canada.
George HarauzBiophysics Interdepartmental Group, University of Guelph, Guelph, ON, Canada.
Leonid S BrownDepartment of Physics, University of Guelph, Guelph, ON, Canada.
Vladimir LadizhanskyDepartment of Physics, University of Guelph, Guelph, ON, Canada. vladizha@uoguelph.ca.
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Direct proton detection is becoming an increasingly popular method for enhancing sensitivity in solid-state nuclear magnetic resonance spectroscopy. Generally, these experiments require extensive deuteration of the protein, fast magic angle spinning (MAS), or a combination of both. Here, we implement direct proton detection to selectively observe the mobile entities in fully-protonated membrane proteins at moderate MAS frequencies. We demonstrate this method on two proteins that exhibit different motional regimes. Myelin basic protein is an intrinsically-disordered, peripherally membrane-associated protein that is highly flexible, whereas Anabaena sensory rhodopsin is composed of seven rigid transmembrane α-helices connected by mobile loop regions. In both cases, we observe narrow proton linewidths and, on average, a 10× increase in sensitivity in 2D insensitive nuclear enhancement of polarization transfer-based HSQC experiments when proton detection is compared to carbon detection. We further show that our proton-detected experiments can be easily extended to three dimensions and used to build complete amino acid systems, including sidechain protons, and obtain inter-residue correlations. Additionally, we detect signals which do not correspond to amino acids, but rather to lipids and/or carbohydrates which interact strongly with membrane proteins.

Indexed as

AnabaenaAnimalsBacterial ProteinsMiceModels, MolecularMyelin Basic ProteinNuclear Magnetic Resonance, BiomolecularProtein ConformationProtonsRhodopsinSignal-To-Noise RatioBacterial ProteinsMyelin Basic ProteinProtonsRhodopsinINEPTJ-couplingsMagic angle spinning (MAS)Membrane proteinsProton detectionSolid-state nuclear magnetic resonance (SSNMR)

Identifiers

PMID26494649
OpenAlexW2177560568

What OpenQuestion holds

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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.