Evidence map›Paper›PMID 24888581›Full record

ArticleJournal of the American Chemical Society2014

Probing water density and dynamics in the chaperonin GroEL cavity.

John M Franck, Miri Sokolovski, Naama Kessler, Erez Matalon, Michal Gordon-Grossman, Song-I Han, Daniella Goldfarb, Amnon Horovitz

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Single-molecule nanopore enzymology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  11. Article
  12. Article
  13. Anomalously Rapid Hydration Water Diffusion Dynamics Near DNA Surfaces.Journal of the American Chemical Society · 2015
    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

8 authors at 1 institution in 1 country.

John M FranckDepartment of Chemistry and Biochemistry, University of California Santa Barbara, California 93106, United States.
Miri Sokolovski
Naama Kessler
Erez Matalon
Michal Gordon-Grossman
Song-I Han
Daniella Goldfarb
Amnon Horovitz
University of California, Santa Barbara · US

Funding

Probing early protein aggregation mechanisms and their relationship to disease efDP2OD008702 · OD · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI HAN, SONGI · 2011 to 2011
$2.3M
NIH HHS DP2 OD008702
6 · The paper itself

Abstract

ATP-dependent binding of the chaperonin GroEL to its cofactor GroES forms a cavity in which encapsulated substrate proteins can fold in isolation from bulk solution. It has been suggested that folding in the cavity may differ from that in bulk solution owing to steric confinement, interactions with the cavity walls, and differences between the properties of cavity-confined and bulk water. However, experimental data regarding the cavity-confined water are lacking. Here, we report measurements of water density and diffusion dynamics in the vicinity of a spin label attached to a cysteine in the Tyr71 → Cys GroES mutant obtained using two magnetic resonance techniques: electron-spin echo envelope modulation and Overhauser dynamic nuclear polarization. Residue 71 in GroES is fully exposed to bulk water in free GroES and to confined water within the cavity of the GroEL-GroES complex. Our data show that water density and translational dynamics in the vicinity of the label do not change upon complex formation, thus indicating that bulk water-exposed and cavity-confined GroES surface water share similar properties. Interestingly, the diffusion dynamics of water near the GroES surface are found to be unusually fast relative to other protein surfaces studied. The implications of these findings for chaperonin-assisted folding mechanisms are discussed.

Indexed as

Base SequenceChaperonin 10Chaperonin 60Electron Spin Resonance SpectroscopyEscherichia coli ProteinsModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein FoldingSpin LabelsWaterChaperonin 10Chaperonin 60Escherichia coli ProteinsSpin LabelsWater

Identifiers

PMID24888581
PMCPMC4091268
OpenAlexW2319417801

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.