Evidence map›Paper›PMID 22379959›Full record

ArticleThe journal of physical chemistry. B2012

Distance measurements on a dual-labeled TOAC AChR M2δ peptide in mechanically aligned DMPC bilayers via dipolar broadening CW-EPR spectroscopy.

Harishchandra Ghimire, Eric J Hustedt, Indra D Sahu, Johnson J Inbaraj, Robert McCarrick, Daniel J Mayo, Monica R Benedikt, Ryan T Lee, Stuart M Grosser, Gary A Lorigan

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  11. Biophysical EPR Studies Applied to Membrane Proteins.Journal of physical chemistry & biophysics
    Article
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

10 authors at 2 institutions in 1 country.

Harishchandra GhimireDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.
Eric J Hustedt
Indra D Sahu
Johnson J Inbaraj
Robert McCarrick
Daniel J Mayo
Monica R Benedikt
Ryan T Lee
Stuart M Grosser
Gary A Lorigan
Miami University · USVanderbilt University · US

Funding

Protein Structure and Dynamics from EPR Spectroscopy and MD SimulationsP01GM080513 · NIGMS · VANDERBILT UNIVERSITY · PI LYBRAND, TERRY P · 2008 to 2012
$5.6M
EPR and Solid-State NMR Studies of Integral Membrane ProteinsR01GM080542 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2007 to 2011
$1.6M
MAGNETIC RESONANCE STUDIES OF MEMBRANE PROTEINSR15GM060259 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2000 to 2000
$105k
NIGMS NIH HHS GM080513NIGMS NIH HHS GM60259-01NIGMS NIH HHS R01 GM080542
6 · The paper itself

Abstract

A membrane alignment technique has been used to measure the distance between two TOAC nitroxide spin labels on the membrane-spanning M2δ, peptide of the nicotinic acetylcholine receptor (AChR), via CW-EPR spectroscopy. The TOAC-labeled M2δ peptides were mechanically aligned using DMPC lipids on a planar quartz support, and CW-EPR spectra were recorded at specific orientations. Global analysis in combination with rigorous spectral simulation was used to simultaneously analyze data from two different sample orientations for both single- and double-labeled peptides. We measured an internitroxide distance of 14.6 Å from a dual TOAC-labeled AChR M2δ peptide at positions 7 and 13 that closely matches with the 14.5 Å distance obtained from a model of the labeled AChR M2δ peptide. In addition, the angles determining the relative orientation of the two nitroxides have been determined, and the results compare favorably with molecular modeling. The global analysis of the data from the aligned samples gives much more precise estimates of the parameters defining the geometry of the two labels than can be obtained from a randomly dispersed sample.

Indexed as

Electron Spin Resonance SpectroscopyAmino Acid SequenceCyclic N-OxidesDimyristoylphosphatidylcholineLipid BilayersModels, ChemicalMolecular Sequence DataPeptidesReceptors, Nicotinic2,2,6,6-tetramethylpiperidine-N-oxide-4-amino-4-carboxylic acidCyclic N-OxidesDimyristoylphosphatidylcholineLipid BilayersPeptidesReceptors, Nicotinic

Identifiers

PMID22379959
PMCPMC3322368
OpenAlexW1964981541

What OpenQuestion holds

Textmetadata
LicenceTDM
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.