Evidence map›Paper›PMID 24145407›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy.

Gabriel Žoldák, Johannes Stigler, Benjamin Pelz, Hongbin Li, Matthias Rief

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Roquin exhibits opposing effects on RNA stem-loop stability through its two ROQ domain binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Prediction of the Stability of Protein Substructures Using AI/ML Techniques.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Molecular Tension Sensors: Moving Beyond Force.Current opinion in biomedical engineering · 2019
    Article
  15. Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Review
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.

Gabriel ŽoldákPhysik Department E22, Technische Universität München, 85748 Garching, Germany.
Johannes Stigler
Benjamin Pelz
Hongbin Li
Matthias Rief

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study we expand the accessible dynamic range of single-molecule force spectroscopy by optical tweezers to the microsecond range by fast sampling. We are able to investigate a single molecule for up to 15 min and with 300-kHz bandwidth as the protein undergoes tens of millions of folding/unfolding transitions. Using equilibrium analysis and autocorrelation analysis of the time traces, the full energetics as well as real-time kinetics of the ultrafast folding of villin headpiece 35 and a stable asparagine 68 alanine/lysine 70 methionine variant can be measured directly. We also performed Brownian dynamics simulations of the response of the bead-DNA system to protein-folding fluctuations. All key features of the force-dependent deflection fluctuations could be reproduced: SD, skewness, and autocorrelation function. Our measurements reveal a difference in folding pathway and cooperativity between wild-type and stable variant of headpiece 35. Autocorrelation force spectroscopy pushes the time resolution of single-molecule force spectroscopy to ∼10 µs thus approaching the timescales accessible for all atom molecular dynamics simulations.

Indexed as

Models, BiologicalProtein FoldingAmino Acid SequenceChromatography, GelCircular DichroismEscherichia coliFluorescenceHumansKineticsMicrofilament ProteinsMolecular Dynamics SimulationMolecular Sequence DataMutationOptical TweezersSpectrum AnalysisThermodynamicsMicrofilament ProteinsvillinChevron plotLangevin equationMarkov modeloptical trappingthermodynamics

Identifiers

PMID24145407
PMCPMC3831443

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.