Evidence map›Paper›PMID 30762170›Full record

ArticleJournal of biomolecular NMR2019

Alpha protons as NMR probes in deuterated proteins.

Kumar Tekwani Movellan, Eszter E Najbauer, Supriya Pratihar, Michele Salvi, Karin Giller, Stefan Becker, Loren B Andreas

Open access · hybridAbstract read
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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein deuterationChemical communications (Cambridge, England) · 2024
    Article
  6. Article
  7. Chemical reviews · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021
    Article
  15. Article
  16. Accessing Methyl Groups in Proteins viaScientific reports · 2019
    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.

Kumar Tekwani MovellanDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Eszter E NajbauerDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Supriya PratiharDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Michele SalviDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Karin GillerDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Stefan BeckerDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.ORCID http://orcid.org/0000-0003-2041-5740
Loren B AndreasDepartment of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany. land@nmr.mpibpc.mpg.de.ORCID http://orcid.org/0000-0003-3216-9065
Max Planck Institute for Biophysical Chemistry · DE

Funding

deutsche forschungsgemeinschaft Emmy Noether program grant AN1316/1-1deutsche forschungsgemeinschaft INST 186/794-3
6 · The paper itself

Abstract

We describe a new labeling method that allows for full protonation at the backbone Hα position, maintaining protein side chains with a high level of deuteration. We refer to the method as alpha proton exchange by transamination (α-PET) since it relies on transaminase activity demonstrated here using Escherichia coli expression. We show that α-PET labeling is particularly useful in improving structural characterization of solid proteins by introduction of an additional proton reporter, while eliminating many strong dipolar couplings. The approach benefits from the high sensitivity associated with 1.3 mm samples, more abundant information including Hα resonances, and the narrow proton linewidths encountered for highly deuterated proteins. The labeling strategy solves amide proton exchange problems commonly encountered for membrane proteins when using perdeuteration and backexchange protocols, allowing access to alpha and all amide protons including those in exchange-protected regions. The incorporation of Hα protons provides new insights, as the close Hα-Hα and Hα-H

Indexed as

DeuteriumProtonsIsotope LabelingMembrane ProteinsMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProteinsVoltage-Dependent Anion Channel 1DeuteriumMembrane ProteinsProteinsProtonsVDAC1 protein, humanVoltage-Dependent Anion Channel 1Isotopic labelingL-Amino acid oxidaseMembrane proteinsNMRStructural restraintsTransamination

Identifiers

PMID30762170
PMCPMC6441447
OpenAlexW2921323684

What OpenQuestion holds

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LicenceCC BY
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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.