Evidence map›Paper›PMID 19483692›Full record

ArticleNature methods2009

Reaching the protein folding speed limit with large, sub-microsecond pressure jumps.

Charles Dumont, Tryggvi Emilsson, Martin Gruebele

Abstract readValidation Study
PubMed Publisher
In one paragraph

Article in Nature methods, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. MonitoringJournal of the American Chemical Society · 2018
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  10. Article
  11. Article
  12. Review
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  14. Review
  15. Fast-folding proteins under stress.Cellular and molecular life sciences : CMLS · 2015
    Review
  16. Article
  17. Role of solvation in pressure-induced helix stabilization.The Journal of chemical physics · 2014
    Article
  18. Review
  19. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Charles DumontDepartment of Physics, University of Illinois, Urbana, Illinois, USA.
Tryggvi Emilsson
Martin Gruebele

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecules are highly pressure-sensitive, but their dynamics upon return to ambient pressure are often too fast to observe with existing approaches. We describe a sample-efficient method capable of large and very fast pressure drops (<1 nanomole, >2,500 atmospheres and <0.7 microseconds). We validated the method by fluorescence-detected refolding of a genetically engineered lambda repressor mutant from its pressure-denatured state. We resolved barrierless structure formation upon return to ambient pressure; we observed a 2.1 +/- 0.7 microsecond refolding time, which is very close to the 'speed limit' for proteins and much faster than the corresponding temperature-jump refolding of the same protein. The ability to experimentally perform a large and very fast pressure drop opens up a new region of the biomolecular energy landscape for atomic-level simulation.

Indexed as

Protein FoldingBiophysical PhenomenaBiophysicsMiniaturizationPressureProtein DenaturationRepressor ProteinsThermodynamicsTime FactorsViral Regulatory and Accessory Proteinsphage repressor proteinsRepressor ProteinsViral Regulatory and Accessory Proteins

Identifiers

PMID19483692

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.