Evidence map›Paper›PMID 24157546›Full record

ArticleNature protocols2013

Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.

Nabanita Das, Dylan T Murray, Timothy A Cross

Abstract read
In one paragraph

Article in Nature protocols, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Journal of the American Chemical Society · 2025
    Article
  4. Review
  5. bioRxiv : the preprint server for biology · 2025
    Article
  6. Expanding the Toolset of Biomolecular NMR with Efficient and Cost-EffectiveChemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  7. Article
  8. Review
  9. 3D-Printable centrifugal devices for biomolecular solid state NMR rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  10. Review
  11. Chemical reviews · 2022
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018
    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

3 authors.

Nabanita Das1] Institute of Molecular Biophysics (IMB), Florida State University (FSU), Tallahassee, Florida, USA. [2] National High Magnetic Field Laboratory (NMHFL), FSU, Tallahassee, Florida, USA.
Dylan T Murray
Timothy A Cross

Funding

Target IdentificationP01AI074805 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2009 to 2013
$8.7M
DYNAMIC AND STRUCTURAL ELUCIDATION OF GRAMICIDIN A'R01AI023007 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 1987 to 2014
$5.1M
Four Mtb Membrane Proteins: Structure and FunctionR01AI073891 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2008 to 2012
$2.0M
NIAID NIH HHS AI 023007NIAID NIH HHS AI 073891NIAID NIH HHS AI 074805NIAID NIH HHS P01 AI074805NIAID NIH HHS R01 AI023007NIAID NIH HHS R01 AI073891
6 · The paper itself

Abstract

Solid-state NMR spectroscopy has been used successfully for characterizing the structure and dynamics of membrane proteins as well as their interactions with other proteins in lipid bilayers. Such an environment is often necessary for achieving native-like structures. Sample preparation is the key to this success. Here we present a detailed description of a robust protocol that results in high-quality membrane protein samples for both magic-angle spinning and oriented-sample solid-state NMR. The procedure is demonstrated using two proteins: CrgA (two transmembrane helices) and Rv1861 (three transmembrane helices), both from Mycobacterium tuberculosis. The success of this procedure relies on two points. First, for samples for both types of NMR experiment, the reconstitution of the protein from a detergent environment to an environment in which it is incorporated into liposomes results in 'complete' removal of detergent. Second, for the oriented samples, proper dehydration followed by rehydration of the proteoliposomes is essential. By using this protocol, proteoliposome samples for magic-angle spinning NMR and uniformly aligned samples (orientational mosaicity of <1°) for oriented-sample NMR can be obtained within 10 d.

Indexed as

Bacterial ProteinsCloning, MolecularLipid BilayersLiposomesMembrane ProteinsMembranes, ArtificialMycobacterium tuberculosisNuclear Magnetic Resonance, BiomolecularTranscription FactorsBacterial ProteinsCrgA protein, Neisseria meningitidisLipid BilayersLiposomesMembrane ProteinsMembranes, ArtificialTranscription Factors

Identifiers

PMID24157546
PMCPMC4107459

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Registered trials

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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.