Evidence map›Paper›PMID 33582999›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

PELDOR/DEER: An Electron Paramagnetic Resonance Method to Study Membrane Proteins in Lipid Bilayers.

Martin F Peter, Kiran Bountra, Konstantinos Beis, Gregor Hagelueken

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 21% 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

3 citing papers in PubMed, 1 citations in OpenAlex.

  1. Review
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. 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

4 authors at 2 institutions in 2 countries.

Martin F PeterInstitute of Structural Biology, Biomedical Center, University of Bonn, Bonn, Germany.
Kiran BountraDepartment of Life Sciences, Imperial College London, London, UK.
Konstantinos BeisDepartment of Life Sciences, Imperial College London, London, UK.
Gregor HageluekenInstitute of Structural Biology, Biomedical Center, University of Bonn, Bonn, Germany. hagelueken@uni-bonn.de.
Research Complex at Harwell · GBUniversity of Bonn · DE

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MR/N020103/1
6 · The paper itself

Abstract

Every membrane protein is involved in close interactions with the lipid environment of cellular membranes. The annular lipids, that are in direct contact with the polypeptide, can in principle be seen as an integral part of its structure, akin to the first hydration shell of soluble proteins. It is therefore desirable to investigate the structure of membrane proteins and especially their conformational flexibility under conditions that are as close as possible to their native state. This can be achieved by reconstituting the protein into proteoliposomes, nanodiscs, or bicelles. In recent years, PELDOR/DEER spectroscopy has proved to be a very useful method to study the structure and function of membrane proteins in such artificial membrane environments. The technique complements both X-ray crystallography and cryo-EM and can be used in combination with virtually any artificial membrane environment and under certain circumstances even in native membranes. Of the above-mentioned membrane mimics, bicelles are currently the least often used for PELDOR studies, although they offer some advantages, especially their ease of use. Here, we provide a step-by-step protocol for studying a bicelle reconstituted membrane protein with PELDOR/DEER spectroscopy.

Indexed as

Spin LabelsATP-Binding Cassette TransportersCell MembraneElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsLipid BilayersMolecular ConformationATP-Binding Cassette TransportersEscherichia coli ProteinsLipid BilayersMcjD protein, E coliSpin LabelsBicelleDEEREPRMembrane proteinPELDOR

Identifiers

PMID33582999
OpenAlexW3129925094

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.