Evidence map›Paper›PMID 17704167›Full record

ArticleBiophysical journal2007

Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes.

Derek Marsh

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

136 citing papers in PubMed, 355 citations in OpenAlex.

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76 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Derek MarshMax-Planck-Institut für biophysikalische Chemie, Abt. Spektroskopie, Göttingen, Germany. dmarsh@gwdg.de
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid-protein interactions are an important determinant of the stability and function of integral and transmembrane proteins. In addition to local interactions at the lipid-protein interface, global interactions such as the distribution of internal lateral pressure may also influence protein conformation. It is shown here that the effects of the membrane lateral pressure profile on the conformation or insertion of proteins in membranes are equivalent to the elastic response to the frustrated spontaneous curvature, c(o), of the component lipid monolayer leaflets. The chemical potential of the protein in the membrane is predicted to depend linearly on the spontaneous curvature of the lipid leaflets, just as does the contribution of the protein to the elastic bending energy of the lipid, and to be independent of the hydrophobic tension, gamma(phob), at the lipid-water interface. Analysis of the dependence of protein partitioning or conformational transitions on spontaneous curvature of the constituent lipids gives an experimental estimate for the cross-sectional intramembrane shape of the protein or its difference between conformations. Values in the region of 50-110 A(2) are estimated for the effective cross-sectional shape changes on the insertion and conductance transitions of alamethicin, and on the activation of CTP:phosphocholine cytidylyltransferase or rhodopsin in lipid membranes. Much larger values are estimated for the mechanosensitive channel, MscL. Values for the change in intramembrane shape may also be used, together with determinations of lipid relative association constants, to estimate contributions of direct lipid-protein interactions to the lateral pressure experienced by the protein. Changes in chemical potential approximately 12 kJ mol(-1) can be estimated for radial changes of 1 A in a protein of diameter 40 A.

Indexed as

Membrane FluidityModels, ChemicalModels, MolecularComputer SimulationLipid BilayersMembrane ProteinsPressureProtein ConformationSurface TensionLipid BilayersMembrane Proteins

Identifiers

PMID17704167
PMCPMC2084255
OpenAlexW2045155470

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.