Evidence map›Paper›PMID 18556516›Full record

ArticleScience (New York, N.Y.)2008

Micelles protect membrane complexes from solution to vacuum.

Nelson P Barrera, Natalie Di Bartolo, Paula J Booth, Carol V Robinson

Abstract read
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In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing 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

166 citing papers in PubMed.

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106 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Nelson P BarreraDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK.
Natalie Di Bartolo
Paula J Booth
Carol V Robinson

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The ability to maintain interactions between soluble protein subunits in the gas phase of a mass spectrometer gives critical insight into the stoichiometry and interaction networks of protein complexes. Conversely, for membrane protein complexes in micelles, the transition into the gas phase usually leads to the disruption of interactions, particularly between cytoplasmic and membrane subunits, and a mass spectrum dominated by large aggregates of detergent molecules. We show that by applying nanoelectrospray to a micellar solution of a membrane protein complex, the heteromeric adenosine 5'-triphosphate (ATP)-binding cassette transporter BtuC2D2, we can maintain the complex intact in the gas phase of a mass spectrometer. Dissociation of either transmembrane (BtuC) or cytoplasmic (BtuD) subunits uncovers modifications to the transmembrane subunits and cooperative binding of ATP. By protecting a membrane protein complex within a n-dodecyl-beta-d-maltoside micelle, we demonstrated a powerful strategy that will enable the subunit stoichiometry and ligand-binding properties of membrane complexes to be determined directly, by precise determination of the masses of intact complexes and dissociated subunits.

Indexed as

MicellesSpectrometry, Mass, Electrospray IonizationAdenosine TriphosphateATP-Binding Cassette TransportersDetergentsEscherichia coli ProteinsGasesGlucosidesHydrophobic and Hydrophilic InteractionsLigandsMultiprotein ComplexesNanotechnologyProtein ConformationProtein Structure, SecondaryProtein SubunitsSolubilityAdenosine TriphosphateATP-Binding Cassette TransportersBtuC peptide, E coliBtuD peptide, E coliDetergentsdodecyl maltosideEscherichia coli ProteinsGasesGlucosidesLigandsMicellesMultiprotein ComplexesProtein Subunits

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.