Evidence map›Paper›PMID 20303866›Full record

ArticleBiophysical journal2010

Tertiary and secondary structure elasticity of a six-Ig titin chain.

Eric H Lee, Jen Hsin, Eleonore von Castelmur, Olga Mayans, Klaus Schulten

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Molecular insights into titin's A-band.Journal of muscle research and cell motility · 2023
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Obscurin is a semi-flexible molecule in solution.Protein science : a publication of the Protein Society · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Identification of an N-terminal inhibitory extension as the primary mechanosensory regulator of twitchin kinase.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

5 authors.

Eric H LeeCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Jen Hsin
Eleonore von Castelmur
Olga Mayans
Klaus Schulten

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI STONE, JOHN H · 1990 to 2011
$19.8M
Molecular Mechanisms of Cellular MechanicsR01GM073655 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SCHULTEN, KLAUS · 2006 to 2009
$1.0M
NCRR NIH HHS P41 RR005969NCRR NIH HHS P41-RR05969NIGMS NIH HHS R01 GM073655NIGMS NIH HHS R01-GM073655
6 · The paper itself

Abstract

The protein titin functions as a mechanical spring conferring passive elasticity to muscle. Force spectroscopy studies have shown that titin exhibits several regimes of elasticity. Disordered segments bring about a soft, entropic spring-type elasticity; secondary structures of titin's immunoglobulin-like (Ig-) and fibronectin type III-like (FN-III) domains provide a stiff elasticity. In this study, we demonstrate a third type of elasticity due to tertiary structure and involving domain-domain interaction and reorganization along the titin chain. Through 870 ns of molecular dynamics simulations involving 29,000-635,000 atom systems, the mechanical properties of a six-Ig domain segment of titin (I65-I70), for which a crystallographic structure is available, are probed. The results reveal a soft tertiary structure elasticity. A remarkably accurate statistical mechanical description for this elasticity is derived and applied. Simulations also studied the stiff, secondary structure elasticity of the I65-I70 chain due to the unraveling of its domains and revealed how force propagates along the chain during the secondary structure elasticity response.

Indexed as

Models, ChemicalModels, MolecularComputer SimulationConnectinElastic ModulusImmunoglobulin GMuscle ProteinsProtein KinasesProtein Structure, TertiaryConnectinImmunoglobulin GMuscle ProteinsProtein Kinases

Identifiers

PMID20303866
PMCPMC2849065

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.