Evidence map›Paper›PMID 29979594›Full record

ArticleJournal of chemical theory and computation2018

Building Blocks of the Outer Membrane: Calculating a General Elastic Energy Model for β-Barrel Membrane Proteins.

Henry J Lessen, Patrick J Fleming, Karen G Fleming, Alexander J Sodt

Open access · greenAbstract read
In one paragraph

Article in Journal of chemical theory and computation, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. OmpA controls order in the outer membrane and shares the mechanical load.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Physical properties of the bacterial outer membrane.Nature reviews. Microbiology · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.Protein science : a publication of the Protein Society · 2020
    Article
  17. Article
  18. Review
  19. Complex Diffusion in Bacteria.Advances in experimental medicine and biology · 2020
    Review
  20. Review
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 1 country.

Henry J LessenT. C. Jenkins Department of Biophysics , Johns Hopkins University , 3400 N. Charles Street , Baltimore , Maryland 21218 , United States.
Patrick J FlemingT. C. Jenkins Department of Biophysics , Johns Hopkins University , 3400 N. Charles Street , Baltimore , Maryland 21218 , United States.
Karen G FlemingT. C. Jenkins Department of Biophysics , Johns Hopkins University , 3400 N. Charles Street , Baltimore , Maryland 21218 , United States.ORCID http://orcid.org/0000-0001-5417-8830
Alexander J SodtEunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda , Maryland 20892 , United States.ORCID http://orcid.org/0000-0002-5570-8212
Johns Hopkins University · USNational Institutes of Health · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Molecular simulations of lipid curvature stress and its effect on transmembrane proteinsZIAHD008955 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SODT, ALEXANDER · 2016 to 2025
$6.2M
Membrane Protein StabilityR01GM079440 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FLEMING, KAREN G. · 2009 to 2022
$4.1M
Intramural NIH HHS Z99 HD999999Intramural NIH HHS ZIA HD008955NIGMS NIH HHS R01 GM079440NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

The outer membranes of Gram negative bacteria are the first points of contact these organisms make with their environment. Understanding how composition determines the mechanical properties of this essential barrier is of paramount importance. Therefore, we developed a new computational method to measure the elasticity of transmembrane proteins found in the outer membrane. Using all-atom molecular dynamics simulations of these proteins, we apply a set of external forces to mechanically stress the transmembrane β-barrels. Our results from four representative β-barrels show that outer membrane proteins display elastic properties that are approximately 70 to 190 times stiffer than neat lipid membranes. These findings suggest that outer membrane β-barrels are a significant source of mechanical stability in bacteria. Our all-atom approach further reveals that resistance to radial stress is encoded by a general mechanism that includes stretching of backbone hydrogen bonds and tilting of β-strands with respect to the bilayer normal. This computational framework facilitates an increased theoretical understanding of how varying lipid and protein amounts affect the mechanical properties of the bacterial outer membrane.

Indexed as

BacteriaBacterial Outer Membrane ProteinsBiomechanical PhenomenaElasticityHydrogen BondingMolecular Dynamics SimulationProtein Structure, SecondaryStress, MechanicalBacterial Outer Membrane Proteins

Identifiers

PMID29979594
PMCPMC6191857
OpenAlexW2842578025

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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.