Evidence map›Paper›PMID 16126828›Full record

ArticleBiophysical journal2005

Flexible charged macromolecules on mixed fluid lipid membranes: theory and Monte Carlo simulations.

Shelly Tzlil, Avinoam Ben-Shaul

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 63 citations in OpenAlex.

  1. Significance of Receptor Mobility in Multivalent Binding on Lipid Membranes.Angewandte Chemie (International ed. in English) · 2022
    Review
  2. Review
  3. Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Adsorption of proteins on a lipid bilayer.European biophysics journal : EBJ · 2010
    Article
  9. Article
  10. Article
  11. Debye-Hückel theory of mixed charged-zwitterionic lipid layers.The European physical journal. E, Soft matter · 2008
    Article
  12. Article
  13. Article
  14. Article
  15. 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 at 1 institution in 1 country.

Shelly TzlilDepartment of Physical Chemistry and The Fritz Haber Research Center, Hebrew University of Jerusalem, Jerusalem, Israel.
Avinoam Ben-Shaul
Hebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluid membranes containing charged lipids enhance binding of oppositely charged proteins by mobilizing these lipids into the interaction zone, overcoming the concomitant entropic losses due to lipid segregation and lower conformational freedom upon macromolecule adsorption. We study this energetic-entropic interplay using Monte Carlo simulations and theory. Our model system consists of a flexible cationic polyelectrolyte, interacting, via Debye-Hückel and short-ranged repulsive potentials, with membranes containing neutral lipids, 1% tetravalent, and 10% (or 1%) monovalent anionic lipids. Adsorption onto a fluid membrane is invariably stronger than to an equally charged frozen or uniform membrane. Although monovalent lipids may suffice for binding rigid macromolecules, polyvalent counter-lipids (e.g., phosphatidylinositol 4,5 bisphosphate), whose entropy loss upon localization is negligible, are crucial for binding flexible macromolecules, which lose conformational entropy upon adsorption. Extending Rosenbluth's Monte Carlo scheme we directly simulate polymer adsorption on fluid membranes. Yet, we argue that similar information could be derived from a biased superposition of quenched membrane simulations. Using a simple cell model we account for surface concentration effects, and show that the average adsorption probabilities on annealed and quenched membranes coincide at vanishing surface concentrations. We discuss the relevance of our model to the electrostatic-switch mechanism of, e.g., the myristoylated alanine-rich C kinase substrate protein.

Indexed as

AdsorptionAlanineBiophysical PhenomenaBiophysicsCationsCell MembraneComputer SimulationDiffusionElectrolytesEntropyIntracellular Signaling Peptides and ProteinsLipidsMacromolecular SubstancesMembrane ProteinsModels, StatisticalMonte Carlo MethodAlanineCationsElectrolytesIntracellular Signaling Peptides and ProteinsLipidsMacromolecular SubstancesMembrane ProteinsMyristic AcidMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylinositol 4,5-DiphosphatePolymers

Identifiers

PMID16126828
PMCPMC1366795
OpenAlexW2027620887

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.