Evidence map›Paper›PMID 18712874›Full record

ArticleJournal of the American Chemical Society2008

Lipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content.

Olivier Soubias, Shui-Lin Niu, Drake C Mitchell, Klaus Gawrisch

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  5. Special issue for Klaus Gawrisch.Biophysical journal · 2023
    Article
  6. Article
  7. Article
  8. Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021
    Review
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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 1 institution in 1 country.

Olivier SoubiasLaboratory of Membrane Biochemistry and Biophysics, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, Maryland 20892, USA.
Shui-Lin Niu
Drake C Mitchell
Klaus Gawrisch
National Institutes of Health · US

Funding

NMR INVESTIGATIONS OF CELL MEMBRANE STRUCTUREZ01AA000003 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI GAWRISCH, KLAUS · 1993 to 2008
$5.4M
Protein/lipid Interactions &Signal TransductionZ01AA000080 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI MITCHELL, DRAKE CURTIS · 1994 to 2008
$1.7M
Intramural NIH HHS Z01 AA000003Intramural NIH HHS Z99 AA999999
6 · The paper itself

Abstract

The ability of photoactivated rhodopsin to achieve the enzymatically active metarhodopsin II conformation is exquisitely sensitive to bilayer hydrophobic thickness. The sensitivity of rhodopsin to the lipid matrix has been explained by the hydrophobic matching theory, which predicts that lipid bilayers adjust elastically to the hydrophobic length of transmembrane helices. Here, we examined if bilayer thickness adjusts to the length of the protein or if the protein alters its conformation to adapt to the bilayer. Purified bovine rhodopsin was reconstituted into a series of mono-unsaturated phosphatidylcholines with 14-20 carbons per hydrocarbon chain. Changes of hydrocarbon chain length were measured by (2)H NMR, and protein helical content was quantified by synchrotron radiation circular dichroism and conventional circular dichroism. Experiments were conducted on dark-adapted rhodopsin, the photo-intermediates metarhodopsin I/II/III, and opsin. Changes of bilayer thickness upon rhodopsin incorporation and photoactivation were mostly absent. In contrast, the helical content of rhodopsin increased with membrane hydrophobic thickness. Helical content did not change measurably upon photoactivation. The increases of bilayer thickness and helicity of rhodopsin are accompanied by higher metarhodopsin II/metarhodopsin I ratios, faster rates of metarhodopsin II formation, an increase of tryptophan fluorescence, and higher temperatures of rhodopsin denaturation. The data suggest a surprising adaptability of this G protein-coupled membrane receptor to properties of the lipid matrix.

Indexed as

AnimalsCattleCircular DichroismHydrophobic and Hydrophilic InteractionsKineticsLipid BilayersNuclear Magnetic Resonance, BiomolecularPhosphatidylcholinesPhotolysisProtein DenaturationProtein Structure, SecondaryRhodopsinSpectrometry, FluorescenceSpectrophotometry, UltravioletTryptophanLipid BilayersPhosphatidylcholinesRhodopsinTryptophan

Identifiers

PMID18712874
PMCPMC2538621
OpenAlexW1964810993

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.