Evidence map›Paper›PMID 10545343›Full record

ArticleBiophysical journal1999

Molecular dynamics of synthetic leucine-serine ion channels in a phospholipid membrane.

H S Randa, L R Forrest, G A Voth, M S Sansom

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 47 citations in OpenAlex.

  1. Transcendent Aspects of Proton Channels.Annual review of physiology · 2024
    Review
  2. Review
  3. Quarterly reviews of biophysics · 2020
    Review
  4. Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  5. Article
  6. Article
  7. Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014
    Review
  8. Benchmark Study of the SCC-DFTB Approach for a Biomolecular Proton Channel.Journal of chemical theory and computation · 2014
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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  17. 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 2 institutions in 2 countries.

H S RandaDepartment of Chemistry and Henry Eyring Center for Theoretical Chemistry, University of Utah, Salt Lake City, Utah 84112-0850, USA.
L R Forrest
G A Voth
M S Sansom
University of Oxford · GBUniversity of Utah · US

Funding

SIMULATIONS OF PROTON TRANSLOCATION IN BIOMOLECULESR01GM053148 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 1996 to 2021
$5.3M
NIGMS NIH HHS GM-53148Wellcome Trust
6 · The paper itself

Abstract

Molecular dynamics calculations were carried out on models of two synthetic leucine-serine ion channels: a tetrameric bundle with sequence (LSLLLSL)(3)NH(2) and a hexameric bundle with sequence (LSSLLSL)(3)NH(2). Each protein bundle is inserted in a palmitoyloleoylphosphatidylcholine bilayer membrane and solvated by simple point charge water molecules inside the pore and at both mouths. Both systems appear to be stable in the absence of an electric field during the 4 ns of molecular dynamics simulation. The water motion in the narrow pore of the four-helix bundle is highly restricted and may provide suitable conditions for proton transfer via a water wire mechanism. In the wider hexameric pore, the water diffuses much more slowly than in bulk but is still mobile. This, along with the dimensions of the pore, supports the observation that this peptide is selective for monovalent cations. Reasonable agreement of predicted conductances with experimentally determined values lends support to the validity of the simulations.

Indexed as

LeucineMolecular Dynamics SimulationSerineAmino Acid SequenceCell MembraneIon ChannelsMolecular Sequence DataPhosphatidylcholinesPorosityProtein Structure, SecondarySubstrate SpecificityWater1-palmitoyl-2-oleoylphosphatidylcholineIon ChannelsLeucinePhosphatidylcholinesSerineWater

Identifiers

PMID10545343
PMCPMC1300517
OpenAlexW2053478600

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.