Evidence map›Paper›PMID 8804611›Full record

ArticleBiophysical journal1996

Surface plasmon resonance spectroscopy studies of membrane proteins: transducin binding and activation by rhodopsin monitored in thin membrane films.

Z Salamon, Y Wang, J L Soulages, M F Brown, G Tollin

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  11. Membrane functional organisation and dynamic of mu-opioid receptors.Cellular and molecular life sciences : CMLS · 2009
    Review
  12. Isolation and functional characterization of a stable complex between photoactivated rhodopsin and the G protein, transducin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  13. Lipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content.Journal of the American Chemical Society · 2008
    Article
  14. Article
  15. Review
  16. 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

5 authors at 1 institution in 1 country.

Z SalamonDepartment of Biochemistry, University of Arizona, Tucson 85721, USA.
Y Wang
J L Soulages
M F Brown
G Tollin
University of Arizona · US

Funding

MEMBRANE BASIS OF VISUAL EXCITATIONR01EY003754 · NEI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BROWN, MICHAEL F · 1985 to 1991
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BIOLOGICAL FUNCTIONS OF ESSENTIAL FATTY ACIDSR01EY010622 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 1994 to 1996
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NEI NIH HHS EY03754NEI NIH HHS EY10622
6 · The paper itself

Abstract

Surface plasmon resonance (SPR) spectroscopy can provide useful information regarding average structural properties of membrane films supported on planar solid substrates. Here we have used SPR spectroscopy for the first time to monitor the binding and activation of G-protein (transducin or Gt) by bovine rhodopsin incorporated into an egg phosphatidylcholine bilayer deposited on a silver film. Rhodopsin incorporation into the membrane, performed by dilution of a detergent solution of the protein, proceeds in a saturable manner. Before photolysis, the SPR data show that Gt binds tightly (Keq approximately equal to 60 nM) and with positive cooperativity to rhodopsin in the lipid layer to form a closely packed film. A simple multilayer model yields a calculated average thickness of about 57 A, in good agreement with the structure of Gt. The data also demonstrate that Gt binding saturates at a Gt/rhodopsin ratio of approximately 0.6. Moreover, upon visible light irradiation, characteristic changes occur in the SPR spectrum, which can be modeled by a 6 A increase in the average thickness of the lipid/protein film caused by formation of metarhodopsin II (MII). Upon subsequent addition of GTP, further SPR spectral changes are induced. These are interpreted as resulting from dissociation of the alpha-subunit of Gt, formation of new MII-Gt complexes, and possible conformational changes of Gt as a consequence of complex formation. The above results clearly demonstrate the ability of SPR spectroscopy to monitor interactions among the proteins associated with signal transduction in membrane-bound systems.

Indexed as

AnimalsBiophysical PhenomenaBiophysicsCattleGuanosine TriphosphateIn Vitro TechniquesLightLipid BilayersMembrane ProteinsMembranes, ArtificialProtein BindingRhodopsinSpectrum AnalysisTransducinGuanosine TriphosphateLipid BilayersMembrane ProteinsMembranes, ArtificialRhodopsinTransducin

Identifiers

PMID8804611
PMCPMC1233479
OpenAlexW2061133720

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.