Evidence map›Paper›PMID 11222274›Full record

ArticleBiophysical journal2001

Statistical thermodynamics of membrane bending-mediated protein-protein attractions.

T Chou, K S Kim, G Oster

Abstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Membrane-Mediated Interactions Between Protein Inclusions.Frontiers in molecular biosciences · 2021
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Defining the free-energy landscape of curvature-inducing proteins on membrane bilayers.Physical review. E, Statistical, nonlinear, and soft matter physics · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Self-assembly of photosynthetic membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2010
    Review
  17. Article
  18. Calculation of free energies in fluid membranes subject to heterogeneous curvature fields.Physical review. E, Statistical, nonlinear, and soft matter physics · 2009
    Article
  19. Article
  20. 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

3 authors.

T ChouDepartment of Biomathematics, UCLA School of Medicine, Los Angeles, California 90095, USA. tomchou@ucla.edu
K S Kim
G Oster

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Highly wedge-shaped integral membrane proteins, or membrane-adsorbed proteins can induce long-ranged deformations. The strain in the surrounding bilayer creates relatively long-ranged forces that contribute to interactions with nearby proteins. In contrast, to direct short-ranged interactions such as van der Waal's, hydrophobic, or electrostatic interactions, both local membrane Gaussian curvature and protein ellipticity can induce forces acting at distances of up to a few times their typical radii. These forces can be attractive or repulsive, depending on the proteins' shape, height, contact angle with the bilayer, and a pre-existing local membrane curvature. Although interaction energies are not pairwise additive, for sufficiently low protein density, thermodynamic properties depend only upon pair interactions. Here, we compute pair interaction potentials and entropic contributions to the two-dimensional osmotic pressure of a collection of noncircular proteins. For flat membranes, bending rigidities of approximately 100k(B)T, moderate ellipticities, and large contact angle proteins, we find thermally averaged attractive interactions of order k(B)T. These interactions may play an important role in the intermediate stages of protein aggregation. Numerous biological processes where membrane bending-mediated interactions may be relevant are cited, and possible experiments are discussed.

Indexed as

Models, StatisticalThermodynamicsLipid BilayersMembrane ProteinsModels, MolecularModels, TheoreticalPhotosynthetic Reaction Center Complex ProteinsProtein Structure, SecondaryRhodopseudomonasStatic ElectricityLipid BilayersMembrane ProteinsPhotosynthetic Reaction Center Complex Proteins

Identifiers

PMID11222274
PMCPMC1301305

What OpenQuestion holds

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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.