Evidence map›Paper›PMID 16150962›Full record

ArticleBiophysical journal2005

T-jump infrared study of the folding mechanism of coiled-coil GCN4-p1.

Ting Wang, Wai Leung Lau, William F DeGrado, Feng Gai

Abstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Review
  5. Review
  6. Article
  7. How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Molecular basis of coiled-coil formation.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  15. 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

4 authors.

Ting WangDepartment of Chemistry and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Wai Leung Lau
William F DeGrado
Feng Gai

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Partially folded intermediates have been frequently observed in equilibrium and kinetic protein folding studies. However, folding intermediates that exist at the native side of the rate-limiting step are rather difficult to study because they often evade detection by conventional folding kinetic methods. Here, we demonstrated that a laser-induced temperature-jump method can potentially be used to identify the existence of such post-transition or hidden intermediates. Specifically, we studied two cross-linked variants of GCN4-p1 coiled-coil. The GCN4 leucine zipper has been studied extensively and most of these studies have regarded it as a two-state folder. Our static circular dichroism and infrared data also indicate that the thermal unfolding of these two monomeric coiled-coils can be adequately described by an apparent two-state model. However, their temperature-jump-induced relaxation kinetics exhibit non-monoexponential behavior, dependent upon sequence and temperature. Taken together, our results support a folding mechanism wherein at least one folding intermediate populates behind the main rate-limiting step.

Indexed as

Models, ChemicalModels, MolecularBasic-Leucine Zipper Transcription FactorsComputer SimulationDNA-Binding ProteinsHot TemperatureKineticsProtein FoldingProtein Structure, SecondarySaccharomyces cerevisiae ProteinsSpectrophotometry, InfraredTime FactorsTranscription FactorsBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsGCN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID16150962
PMCPMC1366983

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.