Evidence map›Paper›PMID 20550913›Full record

ArticleBiophysical journal2010

Kinetic hysteresis in collagen folding.

Kazunori Mizuno, Sergei P Boudko, Jürgen Engel, Hans Peter Bächinger

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Deciphering the folding code of collagens.Nature communications · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  10. Article
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  12. Review
  13. Article
  14. Review
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  17. Review
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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 at 3 institutions in 2 countries.

Kazunori MizunoShriners Hospital for Children, Portland, Oregon, USA.
Sergei P Boudko
Jürgen Engel
Hans Peter Bächinger
Oregon Health & Science University · USShriners Hospitals for Children - Portland · USUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The triple helix of collagen shows a steep unfolding transition upon heating, whereas less steep and more gradual refolding is observed upon cooling. The shape of the hysteresis loop depends on the rate of temperature change as well as the peptide concentration. Experimental heating and cooling rates are usually much faster than rates of unfolding and refolding. In this work, collagen model peptides were used to study hysteresis quantitatively. Their unfolding and refolding profiles were recorded at different heating and cooling rates, and at different peptide concentrations. Data were fitted assuming kinetic mechanisms in which three chains combine to a helix with or without an intermediate that acts as a nucleus. A quantitative fit was achieved with the same kinetic model for the forward and backward reactions. Transitions of exogenously trimerized collagen models were also analyzed with a simplified kinetic mechanism. It follows that true equilibrium transitions can only be measured at high concentrations of polypeptide chains with slow scanning rates, for example, 0.1 degrees C/h at 0.25 mM peptide concentration of (Gly-Pro-Pro)(10). (Gly-Pro-4(R)Hyp)(10) folds approximately 2000 times faster than (Gly-Pro-Pro)(10). This was explained by a more stable nucleus, whereas the rate of propagation was almost equal. The analysis presented here can be used to derive kinetic and thermodynamic data for collagenous and other systems with kinetically controlled hysteresis.

Indexed as

Protein FoldingAmino Acid SequenceCalorimetryCollagenHot TemperatureKineticsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein MultimerizationProtein Structure, QuaternaryCollagenPeptide Fragments

Identifiers

PMID20550913
PMCPMC2884267
OpenAlexW2128880998

What OpenQuestion holds

Textmetadata
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.