Evidence map›Paper›PMID 23539118›Full record

ArticleJournal of biomolecular NMR2013

Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE.

James R Banigan, Anindita Gayen, Nathaniel J Traaseth

Abstract read
In one paragraph

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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.

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3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Extensively sparseJournal of biomolecular NMR · 2021
    Article
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  3. De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  4. Article
  5. Afterglow Solid-State NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  6. Article
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  14. EmrE dimerization depends on membrane environment.Biochimica et biophysica acta · 2014
    Article
  15. Article
  16. Article
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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

James R BaniganDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, USA.
Anindita Gayen
Nathaniel J Traaseth

Funding

Structural Topology of a Small Multidrug Resistant Efflux PumpK22AI083745 · NIAID · NEW YORK UNIVERSITY · PI TRAASETH, NATHANIEL J. · 2011 to 2012
$267k
NIAID NIH HHS 5K22AI083745NIAID NIH HHS K22 AI083745
6 · The paper itself

Abstract

Magic-angle-spinning (MAS) solid-state NMR spectroscopy has emerged as a viable method to characterize membrane protein structure and dynamics. Nevertheless, the spectral resolution for uniformly labeled samples is often compromised by redundancy of the primary sequence and the presence of helical secondary structure that results in substantial resonance overlap. The ability to simplify the spectrum in order to obtain unambiguous site-specific assignments is a major bottleneck for structure determination. To address this problem, we used a combination of (15)N reverse labeling, afterglow spectroscopic techniques, and frequency-selective dephasing experiments that dramatically improved the ability to resolve peaks in crowded spectra. This was demonstrated using the polytopic membrane protein EmrE, an efflux pump involved in multidrug resistance. Residues preceding the (15)N reverse labeled amino acid were imaged using a 3D NCOCX afterglow experiment and those following were recorded using a frequency-selective dephasing experiment. Our approach reduced the spectral congestion and provided a sensitive way to obtain chemical shift assignments for a membrane protein where no high-resolution structure is available. This MAS methodology is widely applicable to the study of other polytopic membrane proteins in functional lipid bilayer environments.

Indexed as

AntiportersEscherichia coli ProteinsMagnetic Resonance SpectroscopyModels, BiologicalAntiportersEmrE protein, E coliEscherichia coli Proteins

Identifiers

PMID23539118
PMCPMC3747971

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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.