Evidence map›Paper›PMID 21825161›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin.

Felix Berkemeier, Morten Bertz, Senbo Xiao, Nikos Pinotsis, Matthias Wilmanns, Frauke Gräter, Matthias Rief

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Accelerated Mechanochemistry in Helical Polymers.Angewandte Chemie (International ed. in English) · 2022
    Article
  6. Review
  7. Nanosurgical Manipulation of Titin and Its M-Complex.Nanomaterials (Basel, Switzerland) · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. ACS chemical neuroscience · 2021
    Article
  12. Article
  13. Article
  14. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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

7 authors at 4 institutions in 3 countries.

Felix BerkemeierPhysik Department E22, Technische Universität München, James-Franck-Straße, 85748 Garching, Germany.
Morten Bertz
Senbo Xiao
Nikos Pinotsis
Matthias Wilmanns
Frauke Gräter
Matthias Rief
Chinese Academy of Sciences · CNDeutsches Elektronen-Synchrotron DESY · DETechnical University of Munich · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The highly oriented filamentous protein network of muscle constantly experiences significant mechanical load during muscle operation. The dimeric protein myomesin has been identified as an important M-band component supporting the mechanical integrity of the entire sarcomere. Recent structural studies have revealed a long α-helical linker between the C-terminal immunoglobulin (Ig) domains My12 and My13 of myomesin. In this paper, we have used single-molecule force spectroscopy in combination with molecular dynamics simulations to characterize the mechanics of the myomesin dimer comprising immunoglobulin domains My12-My13. We find that at forces of approximately 30 pN the α-helical linker reversibly elongates allowing the molecule to extend by more than the folded extension of a full domain. High-resolution measurements directly reveal the equilibrium folding/unfolding kinetics of the individual helix. We show that α-helix unfolding mechanically protects the molecule homodimerization from dissociation at physiologically relevant forces. As fast and reversible molecular springs the myomesin α-helical linkers are an essential component for the structural integrity of the M band.

Indexed as

Protein FoldingBiomechanical PhenomenaConnectinKineticsMicroscopy, Atomic ForceMolecular Dynamics SimulationMuscle ProteinsProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryProtein UnfoldingConnectinMuscle Proteins

Identifiers

PMID21825161
PMCPMC3161521
OpenAlexW1969274786

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.