Evidence map›Paper›PMID 20816060›Full record

ArticleBiophysical journal2010

Lateral diffusion of membrane proteins: consequences of hydrophobic mismatch and lipid composition.

Sivaramakrishnan Ramadurai, Ria Duurkens, Victor V Krasnikov, Bert Poolman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

36 citing papers in PubMed, 61 citations in OpenAlex.

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  5. Energetics of the Transmembrane Peptide Sorting by Hydrophobic Mismatch.The journal of physical chemistry letters · 2024
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  10. Review
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  16. Heterodimer Formation of the Homodimeric ABC Transporter OpuA.International journal of molecular sciences · 2021
    Article
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  18. 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 1 institution in 1 country.

Sivaramakrishnan RamaduraiDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre and the Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh, Groningen, The Netherlands.
Ria Duurkens
Victor V Krasnikov
Bert Poolman
University of Groningen · NL

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Biological membranes are composed of a large number lipid species differing in hydrophobic length, degree of saturation, and charge and size of the headgroup. We now present data on the effect of hydrocarbon chain length of the lipids and headgroup composition on the lateral mobility of the proteins in model membranes. The trimeric glutamate transporter (GltT) and the monomeric lactose transporter (LacY) were reconstituted in giant unilamellar vesicles composed of unsaturated phosphocholine lipids of varying acyl chain length (14-22 carbon atoms) and various ratios of DOPE/DOPG/DOPC lipids. The lateral mobility of the proteins and of a fluorescent lipid analog was determined as a function of the hydrophobic thickness of the bilayer (h) and lipid composition, using fluorescence correlation spectroscopy. The diffusion coefficient of LacY decreased with increasing thickness of the bilayer, in accordance with the continuum hydrodynamic model of Saffman-Delbrück. For GltT, the mobility had its maximum at diC18:1 PC, which is close to the hydrophobic thickness of the bilayer in vivo. The lateral mobility decreased linearly with the concentration of DOPE but was not affected by the fraction of anionic lipids from DOPG. The addition of DOPG and DOPE did not affect the activity of GltT. We conclude that the hydrophobic thickness of the bilayer is a major determinant of molecule diffusion in membranes, but protein-specific properties may lead to deviations from the Saffman-Delbrück model.

Indexed as

Hydrophobic and Hydrophilic InteractionsAmino Acid Transport System X-AGDiffusionEscherichia coliEscherichia coli ProteinsGeobacillus stearothermophilusGlycerophospholipidsMembrane ProteinsMembrane Transport ProteinsSpectrometry, FluorescenceSurface PropertiesUnilamellar LiposomesAmino Acid Transport System X-AGEscherichia coli ProteinsGlycerophospholipidslactose permeaseMembrane ProteinsMembrane Transport ProteinsUnilamellar Liposomes

Identifiers

PMID20816060
PMCPMC2931744
OpenAlexW2100727360

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.