Evidence map›Paper›PMID 29539394›Full record

ArticleBiophysical journal2018

Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding.

Anthony Banks, Sanbo Qin, Kevin L Weiss, Christopher B Stanley, Huan-Xiang Zhou

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Structural and Mechanical Dynamics of Polymer Membranes Across Multilength Scales.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

5 authors.

Anthony BanksInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida.
Sanbo QinInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida.
Kevin L WeissBiology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee.
Christopher B StanleyBiology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee.
Huan-Xiang ZhouInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida; Department of Chemistry and Department of Physics, University of Illinois at Chicago, Chicago, Illinois. Electronic address: hzhou43@uic.edu.

Funding

Quantitative, Mechanistic Studies of Biomolecular RecognitionR35GM118091 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Huan-Xiang Zhou · 2016 to 2026
$6.5M
Modeling Crowding and Confinement of Cellular EnvironmentsR01GM088187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 2010 to 2015
$1.6M
NIGMS NIH HHS R01 GM088187NIGMS NIH HHS R35 GM118091
6 · The paper itself

Abstract

Conformational malleability allows intrinsically disordered proteins (IDPs) to respond agilely to their environments, such as nonspecifically interacting with in vivo bystander macromolecules (or crowders). Previous studies have emphasized conformational compaction of IDPs due to steric repulsion by macromolecular crowders, but effects of soft attraction are largely unexplored. Here we studied the conformational ensembles of the IDP FlgM in both polymer and protein crowders by small-angle neutron scattering. As crowder concentrations increased, the mean radius of gyration of FlgM first decreased but then exhibited an uptick. Ensemble optimization modeling indicated that FlgM conformations under protein crowding segregated into two distinct populations, one compacted and one extended. Coarse-grained simulations showed that compacted conformers fit into an interstitial void and occasionally bind to a surrounding crowder, whereas extended conformers snake through interstitial crevices and bind multiple crowders simultaneously. Crowder-induced conformational segregation may facilitate various cellular functions of IDPs.

Indexed as

Bacterial ProteinsBuffersIntrinsically Disordered ProteinsModels, MolecularPolymersProtein ConformationBacterial ProteinsBuffersFlgN protein, BacteriaIntrinsically Disordered ProteinsPolymers

Identifiers

PMID29539394
PMCPMC5883552

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.