Evidence map›Paper›PMID 22953986›Full record

ArticleJournal of the American Chemical Society2012

Mechanical transition from α-helical coiled coils to β-sheets in fibrin(ogen).

Artem Zhmurov, Olga Kononova, Rustem I Litvinov, Ruxandra I Dima, Valeri Barsegov, John W Weisel

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Molecular Creep Induced Fatigue Rupture of Fibrin Clots.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Rupture mechanics of blood clot fibrin fibers: A coarse-grained model study.Journal of the mechanics and physics of solids · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Visualizing molecular deformation in fibrin networks under tensile loadingChemical communications (Cambridge, England) · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Artem ZhmurovDepartment of Chemistry, University of Massachusetts, Lowell, Massachusetts 01854, United States.
Olga Kononova
Rustem I Litvinov
Ruxandra I Dima
Valeri Barsegov
John W Weisel

Funding

STRUCTURAL STUDIES OF BLOOD CLOTTING PROTEINSR01HL030954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 1985 to 2008
$3.0M
Structural origin of fibrin clot mechanical propertiesR01HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2009 to 2012
$1.6M
Structural origin of fibrin clot mechanical propertiesR56HL090774 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 2014 to 2014
$408k
NHLBI NIH HHS HL030954NHLBI NIH HHS HL090774NHLBI NIH HHS R01 HL030954NHLBI NIH HHS R01 HL090774NHLBI NIH HHS R56 HL090774
6 · The paper itself

Abstract

We characterized the α-to-β transition in α-helical coiled-coil connectors of the human fibrin(ogen) molecule using biomolecular simulations of their forced elongation and theoretical modeling. The force (F)-extension (X) profiles show three distinct regimes: (1) the elastic regime, in which the coiled coils act as entropic springs (F < 100-125 pN; X < 7-8 nm); (2) the constant-force plastic regime, characterized by a force-plateau (F ≈ 150 pN; X ≈ 10-35 nm); and (3) the nonlinear regime (F > 175-200 pN; X > 40-50 nm). In the plastic regime, the three-stranded α-helices undergo a noncooperative phase transition to form parallel three-stranded β-sheets. The critical extension of the α-helices is 0.25 nm, and the energy difference between the α-helices and β-sheets is 4.9 kcal/mol per helical pitch. The soft α-to-β phase transition in coiled coils might be a universal mechanism underlying mechanical properties of filamentous α-helical proteins.

Indexed as

FibrinFibrinogenModels, MolecularProtein ConformationProtein DenaturationFibrinFibrinogen

Identifiers

PMID22953986
PMCPMC3526676

What OpenQuestion holds

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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.