Evidence map›Paper›PMID 20355290›Full record

ArticlePhysical chemistry chemical physics : PCCP2010

Macromolecular crowding induces polypeptide compaction and decreases folding cooperativity.

Douglas Tsao, Nikolay V Dokholyan

Abstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. MACRO-MOLECULAR CROWDING FAVORS WRITHE IN UNWOUND DNA.bioRxiv : the preprint server for biology · 2026
    Article
  2. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
  3. Peptide-based drug design using generative AI.Chemical communications (Cambridge, England) · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Protein folding in the cell: challenges and progress.Current opinion in structural biology · 2011
    Review
  16. 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.

Douglas TsaoDepartment of Chemistry, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.
Nikolay V Dokholyan

Funding

Protein Misfolding and AggregationR01GM080742 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOKHOLYAN, NIKOLAY · 2007 to 2015
$2.8M
NIGMS NIH HHS R01 GM080742NIGMS NIH HHS R01GM080742
6 · The paper itself

Abstract

A cell's interior is comprised of macromolecules that can occupy up to 40% of its available volume. Such crowded environments can influence the stability of proteins and their rates of reaction. Using discrete molecular dynamics simulations, we investigate how both the size and number of neighboring crowding reagents affect the thermodynamic and folding properties of structurally diverse proteins. We find that crowding induces higher compaction of proteins. We also find that folding becomes less cooperative with the introduction of crowders into the system. The crowders may induce alternative non-native protein conformations, thus creating barriers for protein folding in highly crowded media.

Indexed as

Molecular Dynamics SimulationPeptidesProtein FoldingPeptides

Identifiers

PMID20355290
PMCPMC3050011

What OpenQuestion holds

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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.