Evidence map›Paper›PMID 19118204›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Dynamics of one-state downhill protein folding.

Peng Li, Fabiana Y Oliva, Athi N Naganathan, Victor Muñoz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Predicting and Simulating Mutational Effects on Protein Folding Kinetics.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  2. Article
  3. Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. Article
  6. Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019
    Review
  7. 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
  8. 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
  9. Article
  10. Article
  11. Review
  12. Article
  13. Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Review
  16. Article
  17. Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Probing the origins of two-state folding.The Journal of chemical physics · 2013
    Article
  19. Article
  20. 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

4 authors.

Peng LiDepartment of Chemistry and Biochemistry, and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.
Fabiana Y Oliva
Athi N Naganathan
Victor Muñoz

Funding

New Kinetic Approaches to Investigate Protein FoldingR01GM066800 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI MUNOZ, VICTOR · 2003 to 2007
$1.3M
NIGMS NIH HHS R01 GM066800NIGMS NIH HHS R01-GM066800
6 · The paper itself

Abstract

The small helical protein BBL has been shown to fold and unfold in the absence of a free energy barrier according to a battery of quantitative criteria in equilibrium experiments, including probe-dependent equilibrium unfolding, complex coupling between denaturing agents, characteristic DSC thermogram, gradual melting of secondary structure, and heterogeneous atom-by-atom unfolding behaviors spanning the entire unfolding process. Here, we present the results of nanosecond T-jump experiments probing backbone structure by IR and end-to-end distance by FRET. The folding dynamics observed with these two probes are both exponential with common relaxation times but have large differences in amplitude following their probe-dependent equilibrium unfolding. The quantitative analysis of amplitude and relaxation time data for both probes shows that BBL folding dynamics are fully consistent with the one-state folding scenario and incompatible with alternative models involving one or several barrier crossing events. At 333 K, the relaxation time for BBL is 1.3 micros, in agreement with previous folding speed limit estimates. However, late folding events at room temperature are an order of magnitude slower (20 micros), indicating a relatively rough underlying energy landscape. Our results in BBL expose the dynamic features of one-state folding and chart the intrinsic time-scales for conformational motions along the folding process. Interestingly, the simple self-averaging folding dynamics of BBL are the exact dynamic properties required in molecular rheostats, thus supporting a biological role for one-state folding.

Indexed as

Protein FoldingFluorescence Resonance Energy TransferKineticsMotionProtein DenaturationSpectroscopy, Fourier Transform InfraredTemperature

Identifiers

PMID19118204
PMCPMC2629219

What OpenQuestion holds

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Registered trials

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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.