Evidence map›Paper›PMID 23202987›Full record

ArticleJournal of biomolecular NMR2013

Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.

Birgit Habenstein, Antoine Loquet, Karin Giller, Stefan Becker, Adam Lange

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Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

3 citing papers in PubMed.

  1. Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.Protein science : a publication of the Protein Society · 2015
    Article
  2. Article
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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

5 authors.

Birgit HabensteinDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Antoine Loquet
Karin Giller
Stefan Becker
Adam Lange

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

(13)C spin diluted protein samples can be produced using [1-(13)C] and [2-(13)C]-glucose (Glc) carbon sources in the bacterial growth medium. The (13)C spin dilution results in favorable (13)C spectral resolution and polarization transfer behavior. We recently reported the combined use of [1-(13)C]- and [2-(13)C]-Glc labeling to facilitate the structural analysis of insoluble and non-crystalline biological systems by solid-state NMR (ssNMR), including sequential assignment, detection of long-range contacts and structure determination of macromolecular assemblies. In solution NMR the beneficial properties of sparsely labeled samples using [2-(13)C]-glycerol ((13)C labeled Cα sites on a (12)C diluted background) have recently been exploited to provide a bi-directional assignment method (Takeuchi et al. in J Biomol NMR 49(1):17-26, 2011 ). Inspired by this approach and our own recent results using [2-(13)C]-Glc as carbon sources for the simplification of ssNMR spectra, we present a strategy for a bi-directional sequential assignment of solid-state NMR resonances and additionally the detection of long-range contacts using the combination of (13)C spin dilution and 3D NMR spectroscopy. We illustrate our results with the sequential assignment and the collection of distance restraints on an insoluble and non-crystalline supramolecular assembly, the Salmonella typhimurium type III secretion system needle.

Indexed as

Electron Spin Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularBacterial ProteinsBacterial Secretion SystemsCarbon IsotopesModels, MolecularSalmonella typhimuriumBacterial ProteinsBacterial Secretion SystemsCarbon Isotopes

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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.