Evidence map›Paper›PMID 24930025›Full record

ArticleThe Journal of membrane biology2014

Molecular dynamics simulations of a membrane protein/amphipol complex.

Jason D Perlmutter, Jean-Luc Popot, Jonathan N Sachs

Abstract read
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In one paragraph

Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

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  8. Amphipols for each season.The Journal of membrane biology · 2014
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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

3 authors at 3 institutions in 2 countries.

Jason D PerlmutterDepartment of Physics, Brandeis University, 415 South Street, Waltham, MA, 02453, USA, perlm@brandeis.edu.
Jean-Luc Popot
Jonathan N Sachs
Brandeis University · USLaboratoire de Biologie Physico-Chimique des Protéines Membranaires · FRUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphipathic polymers known as "amphipols" provide a highly stabilizing environment for handling membrane proteins in aqueous solutions. A8-35, an amphipol with a polyacrylate backbone and hydrophobic grafts, has been extensively characterized and widely employed for structural and functional studies of membrane proteins using biochemical and biophysical approaches. Given the sensitivity of membrane proteins to their environment, it is important to examine what effects amphipols may have on the structure and dynamics of the proteins they complex. Here we present the first molecular dynamics study of an amphipol-stabilized membrane protein, using Escherichia coli OmpX as a model. We begin by describing the structure of the complexes formed by supplementing OmpX with increasing amounts of A8-35, in order to determine how the amphipol interacts with the transmembrane and extramembrane surfaces of the protein. We then compare the dynamics of the protein in either A8-35, a detergent, or a lipid bilayer. We find that protein dynamics on all accessible length scales is restrained by A8-35, which provides a basis to understanding some of the stabilizing and functional effects of amphipols that have been experimentally observed.

Indexed as

Molecular Dynamics SimulationBacterial Outer Membrane ProteinsCell MembraneComputer SimulationEscherichia coli ProteinsHydrolasesHydrophobic and Hydrophilic InteractionsLipid BilayersModels, BiologicalModels, ChemicalPolymersPropylaminesProtein ConformationSolubilitySolutionsSurface-Active Agentsamphipol A8-35Bacterial Outer Membrane ProteinsEscherichia coli ProteinsHydrolasesLipid BilayersOmpX protein, E coliPolymersPropylaminesSolutionsSurface-Active AgentsWater

Identifiers

PMID24930025
OpenAlexW1970782847

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.