Evidence map›Paper›PMID 16964530›Full record

ArticleJournal of biomolecular NMR2006

Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. coli cytochrome bo3 oxidase.

Heather L Frericks, Donghua H Zhou, Lai Lai Yap, Robert B Gennis, Chad M Rienstra

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Improving cell-free metabolism through direct integration of artificial respiratory chains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  3. Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  7. TScientific reports · 2019
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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.

Heather L FrericksDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Donghua H Zhou
Lai Lai Yap
Robert B Gennis
Chad M Rienstra

Funding

Structure and Function of Membrane Protein Complexes(RMI)R01GM075937 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RIENSTRA, CHAD M · 2005 to 2009
$1.4M
NIGMS NIH HHS GM075937-01
6 · The paper itself

Abstract

Recent progress in magic-angle spinning (MAS) solid-state NMR (SSNMR) has enabled multidimensional studies of large, macroscopically unoriented membrane proteins with associated lipids, without the requirement of solubility that limits other structural techniques. Here we present initial sample preparation and SSNMR studies of a 144 kDa integral membrane protein, E. coli cytochrome bo(3) oxidase. The optimized protocol for expression and purification yields approximately 5 mg of the enzymatically active, uniformly (13)C,(15)N-enriched membrane protein complex from each liter of growth medium. The preparation retains endogenous lipids and yields spectra of high sensitivity and resolution, consistent with a folded, homogenous protein. Line widths of isolated signals are less than 0.5 ppm, with a large number of individual resonances resolved in the 2D and 3D spectra. The (13)C chemical shifts, assigned by amino acid type, are consistent with the secondary structure previously observed by diffraction methods. Although the structure is predominantly helical, the percentage of non-helical signals varies among residue types; these percentages agree well between the NMR and diffraction data. Samples show minimal evidence of degradation after several weeks of NMR data acquisition. Use of a triple resonance scroll resonator probe further improves sample stability and enables higher power decoupling, higher duty cycles and more advanced 3D experiments to be performed. These initial results in cytochrome bo(3) oxidase demonstrate that multidimensional MAS SSNMR techniques have sufficient sensitivity and resolution to interrogate selected parts of a very large uniformly (13)C,(15)N-labeled membrane protein.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SequenceCarbon IsotopesElectron Transport Complex IVEnzyme StabilityEscherichia coliMass SpectrometryMembrane ProteinsModels, MolecularMolecular WeightNitrogen IsotopesProtein FoldingProtein Structure, SecondarySensitivity and SpecificityTemperatureTime FactorsCarbon IsotopesElectron Transport Complex IVMembrane ProteinsNitrogen Isotopes

Identifiers

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Read underepoch 390

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.