Evidence map›Paper›PMID 14990485›Full record

ArticleBiophysical journal2004

A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles.

Isabelle Marcotte, Frances Separovic, Michèle Auger, Stéphane M Gagné

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 109 citations in OpenAlex.

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  9. Lipid concentration and molar ratio boundaries for the use of isotropic bicelles.Langmuir : the ACS journal of surfaces and colloids · 2014
    Article
  10. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
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  12. Article
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  18. Membrane catalysis of peptide-receptor binding.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010
    Review
  19. Article
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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

4 authors at 2 institutions in 2 countries.

Isabelle MarcotteDépartement de Chimie, Centre de Recherche en Sciences et Ingénierie des Macromolécules, Université Laval, Québec, Québec, Canada, G1K 7P4.
Frances Separovic
Michèle Auger
Stéphane M Gagné
Université Laval · CAUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enkephalins are pentapeptides found in the central nervous system. It is believed that these neuropeptides interact with the nerve cell membrane to adopt a conformation suitable for their binding to an opiate receptor. In this work, we have determined the three-dimensional structure of methionine-enkephalin (Menk) in fast-tumbling bicelles using multidimensional (1)H NMR. Bicelles were selected as model membranes because both their bilayer organization and composition resemble those of natural biomembranes. The effect of the membrane composition on the peptide conformation was explored using both zwitterionic (PC bicelles) and negatively charged bicelles (Bic/PG). Pulsed field gradient experiments allowed the determination of the proportion of Menk bound to the model membranes. Approximately 60% of the water-soluble enkephalin was found to associate to the bicellar systems. Structure calculations from torsion angle and NOE-based distance constraints suggest the presence of both micro - and delta-selective conformers of Menk in each system and slightly different conformers in PC bicelles and Bic/PG. As opposed to previous studies of enkephalins in membrane mimetic systems, our results show that these opiate peptides could adopt several conformations in a membrane environment, which is consistent with the flexibility and poor selectivity of enkephalins.

Indexed as

BiomimeticsCell MembraneColloidsDiffusionEnkephalin, MethionineLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsMembranes, ArtificialMicellesMolecular ConformationMotionPhospholipidsProtein BindingProtein ConformationProtonsColloidsEnkephalin, MethionineLipid BilayersMembrane ProteinsMembranes, ArtificialMicellesPhospholipidsProtons

Identifiers

PMID14990485
PMCPMC1303993
OpenAlexW2052706878

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.