Evidence map›Paper›PMID 20221255›Full record

ArticlePLoS computational biology2010

Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm.

Sean R McGuffee, Adrian H Elcock

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 321 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
321citing papers in PubMed, 1 pooled it
22.7field-weighted citation impact, top 1% 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

321 citing papers in PubMed, 1 synthesis or guideline pooled it, 700 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Exploring the effects of excipients on complex coacervation.Journal of colloid and interface science · 2025
    Article
  6. Article
  7. Mechanisms and Pathological Significance of Liquid-Liquid Phase Separation in Bacteria.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Decoding in-cell respiratory enzyme dynamics by label-free in situ electrochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Macromolecular interactions and geometrical confinement determine the 3D diffusion of ribosome-sized particles in liveProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

261 more citing papers are in PubMed but not listed here.

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.

Sean R McGuffeeDepartment of Biochemistry, University of Iowa, Iowa City, Iowa, United States of America.
Adrian H Elcock
University of Iowa · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A longstanding question in molecular biology is the extent to which the behavior of macromolecules observed in vitro accurately reflects their behavior in vivo. A number of sophisticated experimental techniques now allow the behavior of individual types of macromolecule to be studied directly in vivo; none, however, allow a wide range of molecule types to be observed simultaneously. In order to tackle this issue we have adopted a computational perspective, and, having selected the model prokaryote Escherichia coli as a test system, have assembled an atomically detailed model of its cytoplasmic environment that includes 50 of the most abundant types of macromolecules at experimentally measured concentrations. Brownian dynamics (BD) simulations of the cytoplasm model have been calibrated to reproduce the translational diffusion coefficients of Green Fluorescent Protein (GFP) observed in vivo, and "snapshots" of the simulation trajectories have been used to compute the cytoplasm's effects on the thermodynamics of protein folding, association and aggregation events. The simulation model successfully describes the relative thermodynamic stabilities of proteins measured in E. coli, and shows that effects additional to the commonly cited "crowding" effect must be included in attempts to understand macromolecular behavior in vivo.

Indexed as

Models, ChemicalModels, MolecularComputer SimulationCytoplasmEscherichia coliEscherichia coli ProteinsProtein ConformationProtein FoldingEscherichia coli Proteins

Identifiers

PMID20221255
PMCPMC2832674
OpenAlexW2089102241

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.