Evidence map›Paper›PMID 22363011›Full record

ArticleScience (New York, N.Y.)2012

Single-molecule fluorescence experiments determine protein folding transition path times.

Hoi Sung Chung, Kevin McHale, John M Louis, William A Eaton

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.

0numbers the graph read from it
0cells of the map it votes in
171citing 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

171 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Hierarchical friction memory leads to subdiffusive configurational dynamics of fast-folding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Bayesian Nonparametrics for FRET using Realistic Integrative Detectors.bioRxiv : the preprint server for biology · 2025
    Article
  8. Accelerating Molecular Dynamics through Informed Resetting.Journal of chemical theory and computation · 2025
    Article
  9. Article
  10. Article
  11. Unraveling dynamic protein structures by two-dimensional infrared spectra with a pretrained machine learning model.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Accelerating Kinetics with Time-Reversal Path Sampling.Molecules (Basel, Switzerland) · 2023
    Article

111 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

4 authors.

Hoi Sung ChungLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health (NIH), Bethesda, MD 20892-0520, USA. chunghoi@niddk.nih.gov
Kevin McHale
John M Louis
William A Eaton

Funding

Sickle cell disease molecular pathogenesis and drug therapyZIADK029053 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2009 to 2025
$24.8M
Single Molecule Studies of Protein FoldingZIADK029055 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2009 to 2015
$3.3M
Intramural NIH HHS Z99 DA999999Intramural NIH HHS Z99 DK999999Intramural NIH HHS Z99 OD999999
6 · The paper itself

Abstract

The transition path is the tiny fraction of an equilibrium molecular trajectory when a transition occurs as the free-energy barrier between two states is crossed. It is a single-molecule property that contains all the mechanistic information on how a process occurs. As a step toward observing transition paths in protein folding, we determined the average transition-path time for a fast- and a slow-folding protein from a photon-by-photon analysis of fluorescence trajectories in single-molecule Förster resonance energy transfer experiments. Whereas the folding rate coefficients differ by a factor of 10,000, the transition-path times differ by a factor of less than 5, which shows that a fast- and a slow-folding protein take almost the same time to fold when folding actually happens. A very simple model based on energy landscape theory can explain this result.

Indexed as

Protein FoldingAmino Acid SequenceBacterial ProteinsCarrier ProteinsFatty Acid-Binding ProteinsFluorescence Resonance Energy TransferKineticsLikelihood FunctionsModels, MolecularMolecular Sequence DataPhotonsProtein ConformationProtein Interaction Domains and MotifsProtein Structure, TertiaryThermodynamicsBacterial ProteinsCarrier ProteinsFatty Acid-Binding ProteinsFnbp1 protein, mouseIgG Fc-binding protein, Streptococcus

Identifiers

PMID22363011
PMCPMC3878298

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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.