Evidence map›Paper›PMID 25056406›Full record

ArticleJournal of the American Chemical Society2014

General mechanism of two-state protein folding kinetics.

Geoffrey C Rollins, Ken A Dill

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Origins of Life: The Protein Folding Problem all over again?Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. The prebiotic emergence of biological evolution.Royal Society open science · 2024
    Article
  10. On the role of native contact cooperativity in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Deep mining of the protein energy landscape.Structural dynamics (Melville, N.Y.) · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    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

2 authors.

Geoffrey C RollinsDepartment of Biochemistry and Biophysics, University of California , San Francisco, California 94143, United States.
Ken A Dill

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
NIGMS NIH HHS T32 GM008284
6 · The paper itself

Abstract

We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure. It shows how sequential pathways are consistent with multiple stochastic routes on funnel landscapes, and it gives good agreement with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins, at the same time it is consistent with the near independence of folding equilibrium constant on size. This model gives estimates of folding rates of proteomes, leading to a median folding time in Escherichia coli of about 5 s.

Indexed as

Protein FoldingAnisotropyBiopolymersCamphorDeuterium OxideGraphiteKineticsMagnetic Resonance SpectroscopyMolecular WeightOrganic ChemicalsOxidesProlineProteinsSolutionsSolventsSucroseBiopolymersCamphorDeuterium OxideGraphiteOrganic ChemicalsOxidesProlineProteinsSolutionsSolventsSucrose

Identifiers

PMID25056406
PMCPMC5104671

What OpenQuestion holds

Textmetadata
LicenceTDM
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.