Evidence map›Paper›PMID 16731967›Full record

ArticleProtein science : a publication of the Protein Society2006

Positioning of proteins in membranes: a computational approach.

Andrei L Lomize, Irina D Pogozheva, Mikhail A Lomize, Henry I Mosberg

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed, 1 pooled it
5.7field-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

118 citing papers in PubMed, 1 synthesis or guideline pooled it, 256 citations in OpenAlex.

  1. Pooled it
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  5. A membrane insertion code for intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
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  14. Activation of the influenza B M2 proton channel (BM2).bioRxiv : the preprint server for biology · 2024
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  17. Extracellular Kir2.1Circulation research · 2024
    Article
  18. Article
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  20. Article

58 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

4 authors at 2 institutions in 1 country.

Andrei L LomizeCollege of Pharmacy, University of Michigan, Ann Arbor, Michigan 48109-1065, USA. almz@umich.edu
Irina D Pogozheva
Mikhail A Lomize
Henry I Mosberg
University of Michigan–Ann Arbor · USMichigan Medicine · US

Funding

Development of Mixed Function Opioid Peptides and PeptidomimeticsR01DA003910 · NIDA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MOSBERG, HENRY ISAAC · 1985 to 2017
$9.0M
NIDA NIH HHS DA003910NIDA NIH HHS R01 DA003910
6 · The paper itself

Abstract

A new computational approach has been developed to determine the spatial arrangement of proteins in membranes by minimizing their transfer energies from water to the lipid bilayer. The membrane hydrocarbon core was approximated as a planar slab of adjustable thickness with decadiene-like interior and interfacial polarity profiles derived from published EPR studies. Applicability and accuracy of the method was verified for a set of 24 transmembrane proteins whose orientations in membranes have been studied by spin-labeling, chemical modification, fluorescence, ATR FTIR, NMR, cryo-microscopy, and neutron diffraction. Subsequently, the optimal rotational and translational positions were calculated for 109 transmembrane, five integral monotopic and 27 peripheral protein complexes with known 3D structures. This method can reliably distinguish transmembrane and integral monotopic proteins from water-soluble proteins based on their transfer energies and membrane penetration depths. The accuracies of calculated hydrophobic thicknesses and tilt angles were approximately 1 A and 2 degrees, respectively, judging from their deviations in different crystal forms of the same proteins. The hydrophobic thicknesses of transmembrane proteins ranged from 21.1 to 43.8 A depending on the type of biological membrane, while their tilt angles with respect to the bilayer normal varied from zero in symmetric complexes to 26 degrees in asymmetric structures. Calculated hydrophobic boundaries of proteins are located approximately 5 A lower than lipid phosphates and correspond to the zero membrane depth parameter of spin-labeled residues. Coordinates of all studied proteins with their membrane boundaries can be found in the Orientations of Proteins in Membranes (OPM) database:http://opm.phar.umich.edu/.

Indexed as

Models, MolecularAmino AcidsCell MembraneComputer SimulationDatabases, ProteinHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsProtein ConformationAmino AcidsLipid BilayersMembrane Proteins

Identifiers

PMID16731967
PMCPMC2242528
OpenAlexW2145020089

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.