Evidence map›Paper›PMID 9649403›Full record

ArticleBiophysical journal1998

Protein folding: matching theory and experiment.

D V Laurents, R L Baldwin

Abstract read
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Universality and diversity of folding mechanics for three-helix bundle proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein folding and unfolding on a complex energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  12. Kinetic evidence of an on-pathway intermediate in the folding of lysozyme.Protein science : a publication of the Protein Society · 2000
    Article
  13. Searching for "downhill scenarios" in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Review
  14. Article
  15. A specific transition state for S-peptide combining with folded S-protein and then refolding.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  16. Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

2 authors.

D V LaurentsBiochemistry Department, Beckman Center, Stanford Medical Center, Stanford, California 94305-5307, USA.
R L Baldwin

Funding

PHYSICAL STUDIES OF PROTEINSR01GM019988 · NIGMS · STANFORD UNIVERSITY · PI BALDWIN, ROBERT L · 1985 to 1988
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PROTEIN FOLDING PATHWAYSR37GM019988 · NIGMS · STANFORD UNIVERSITY · PI BALDWIN, ROBERT L · 1988 to 1997
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NIGMS NIH HHS GM 19988
6 · The paper itself

Abstract

The impact of folding funnels and folding simulations on the way experimentalists interpret results is examined. The image of the transition state has changed from a unique species that has a strained configuration, with a correspondingly high free energy, to a more ordinary folding intermediate, whose balance between limited conformational entropy and stabilizing contacts places it at the top of the free energy barrier. Evidence for a broad transition barrier comes from studies showing that mutations can change the position of the barrier. The main controversial issue now is whether populated folding intermediates are productive on-pathway intermediates or dead-end traps. Direct experimental evidence is needed. Theories suggesting that populated intermediates are trapped in a glasslike state are usually based on mechanisms which imply that trapping would only be extremely short-lived (e.g., nanoseconds) in water at 25 degrees C. There seems to be little experimental evidence for long-lived trapping in monomers, if folding aggregates are excluded. On the other hand, there is good evidence for kinetic trapping in dimers. alpha-Helix formation is currently the fastest known process in protein folding, and incipient helices are present at the start of folding. Fast helix formation has the effect of narrowing drastically the choice of folding routes. Thus helix formation can direct folding. It changes the folding metaphor from pouring liquid down a folding funnel to a train leaving a switchyard with only a few choices of exit tracks.

Indexed as

Protein FoldingBiophysical PhenomenaBiophysicsKineticsModels, ChemicalProteinsProtein Structure, SecondaryThermodynamicsProteins

Identifiers

PMID9649403
PMCPMC1299715

What OpenQuestion holds

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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.