Evidence map›Paper›PMID 21152910›Full record

ArticleThe Journal of membrane biology2011

A comparative study on the ability of two implicit solvent lipid models to predict transmembrane helix tilt angles.

Aaron Frank, Ioan Andricioaei

Abstract readComparative Study
In one paragraph

Article in The Journal of membrane biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

2 authors.

Aaron FrankDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Ioan Andricioaei

Funding

SUPPLEMENT FOR MARC SCIENTIFIC COMMUNICATIONS TECHNOLOGYT34GM008078 · NIGMS · BROOKLYN COLLEGE · PI HAINLINE, LOUISE, RABIN, LAURA A. · 1985 to 2022
$8.2M
6 · The paper itself

Abstract

Free-energy profiles describing the relative orientation of membrane proteins along predefined coordinates can be efficiently calculated by means of umbrella simulations. Such simulations generate reliable orientational distributions but are difficult to converge because of the very long equilibration times of the solvent and the lipid bilayer in explicit representation. Two implicit lipid membrane models are here applied in combination with the umbrella sampling strategy to the simulation of the transmembrane (TM) helical segment from virus protein U (Vpu). The models are used to study both orientation and energetics of this α-helical peptide as a function of hydrophobic mismatch. We observe that increasing the degree of positive hydrophobic mismatch increased the tilt angle of Vpu. These findings agree well with experimental data and as such validate the solvation models used in this study.

Indexed as

Computer SimulationModels, BiologicalCell MembraneHydrophobic and Hydrophilic InteractionsLipid BilayersLipidsMembrane ProteinsSolventsLipid BilayersLipidsMembrane ProteinsSolvents

Identifiers

PMID21152910
PMCPMC3030950

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.