Evidence map›Paper›PMID 23149740›Full record

ArticleNature communications2012

Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy.

Alessandro Borgia, Beth G Wensley, Andrea Soranno, Daniel Nettels, Madeleine B Borgia, Armin Hoffmann, Shawn H Pfeil, Everett A Lipman, Jane Clarke, Benjamin Schuler

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 132 citations in OpenAlex.

  1. Article
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  8. The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  9. Article
  10. Theory and Analysis of Single-Molecule FRET Experiments.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

2 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

10 authors at 4 institutions in 4 countries.

Alessandro BorgiaDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Beth G Wensley
Andrea Soranno
Daniel Nettels
Madeleine B Borgia
Armin Hoffmann
Shawn H Pfeil
Everett A Lipman
Jane Clarke
Benjamin Schuler
University of Zurich · CHUniversity of California, Santa Barbara · USUniversity of Cambridge · GBNational Institute for Nanotechnology · CA

Funding

Wellcome Trust 095195Wellcome Trust WT095195MA
6 · The paper itself

Abstract

Theory, simulations and experimental results have suggested an important role of internal friction in the kinetics of protein folding. Recent experiments on spectrin domains provided the first evidence for a pronounced contribution of internal friction in proteins that fold on the millisecond timescale. However, it has remained unclear how this contribution is distributed along the reaction and what influence it has on the folding dynamics. Here we use a combination of single-molecule Förster resonance energy transfer, nanosecond fluorescence correlation spectroscopy, microfluidic mixing and denaturant- and viscosity-dependent protein-folding kinetics to probe internal friction in the unfolded state and at the early and late transition states of slow- and fast-folding spectrin domains. We find that the internal friction affecting the folding rates of spectrin domains is highly localized to the early transition state, suggesting an important role of rather specific interactions in the rate-limiting conformational changes.

Indexed as

FrictionProtein FoldingDiffusionFluorescence Resonance Energy TransferKineticsMicrofluidicsProteinsProtein Structure, TertiarySolventsSpectrinSpectrometry, FluorescenceViscosityProteinsSolventsSpectrin

Identifiers

PMID23149740
PMCPMC3514500
OpenAlexW2082810430

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.