Evidence map›Paper›PMID 24641816›Full record

ReviewQuarterly reviews of biophysics2014

Fast protein folding kinetics.

Hannah Gelman, Martin Gruebele

Open access · greenAbstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 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
3.8field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Review
  12. 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
  13. Article
  14. Article
  15. Review
  16. Article
  17. Downhill, Ultrafast and Fast Folding Proteins Revised.International journal of molecular sciences · 2020
    Article
  18. Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019
    Review
  19. Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

2 authors at 2 institutions in 1 country.

Hannah GelmanDepartments of Physics, Chemistry, and Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA.
Martin GruebeleDepartments of Physics, Chemistry, and Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA.
University of Illinois Urbana-Champaign · USUrbana University · US

Funding

Protein refolding and transient aggregate formation studied by very fast pressureR01GM093318 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GRUEBELE, MARTIN · 2010 to 2020
$3.1M
NIGMS NIH HHS R01 GM093318NIGMS NIH HHS R02 GM093318-4
6 · The paper itself

Abstract

Fast-folding proteins have been a major focus of computational and experimental study because they are accessible to both techniques: they are small and fast enough to be reasonably simulated with current computational power, but have dynamics slow enough to be observed with specially developed experimental techniques. This coupled study of fast-folding proteins has provided insight into the mechanisms, which allow some proteins to find their native conformation well <1 ms and has uncovered examples of theoretically predicted phenomena such as downhill folding. The study of fast folders also informs our understanding of even 'slow' folding processes: fast folders are small; relatively simple protein domains and the principles that govern their folding also govern the folding of more complex systems. This review summarizes the major theoretical and experimental techniques used to study fast-folding proteins and provides an overview of the major findings of fast-folding research. Finally, we examine the themes that have emerged from studying fast folders and briefly summarize their application to protein folding in general, as well as some work that is left to do.

Indexed as

Protein FoldingKineticsModels, MolecularProteinsProteins

Identifiers

PMID24641816
PMCPMC4047647
OpenAlexW2065023288

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.