ArticleBiophysical journal2015
Titin domains progressively unfolded by force are homogenously distributed along the molecule.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- The roles of the microtubule cytoskeletal network in cardiac mechanobiology.Journal of cell science · 2026Review
- Mechanical forces regulate the composition and fate of stalled nascent chains.Molecular cell · 2026Article
- On the free energy of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- On the distance to the transition state of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- An overview of insights and updates on TTN mutations in cardiomyopathies.Frontiers in pharmacology · 2025Review
- Application of optical tweezers in cardiovascular research: More than just a measuring tool.Frontiers in bioengineering and biotechnology · 2022Review
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.International journal of molecular sciences · 2021Article
- Homozygous expression of the myofibrillar myopathy-associated p.W2710X filamin C variant reveals major pathomechanisms of sarcomeric lesion formation.Acta neuropathologica communications · 2020Article
- A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues.Nature communications · 2020Article
- Stretching single titin molecules from failing human hearts reveals titin's role in blunting cardiac kinetic reserve.Cardiovascular research · 2020Article
- Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity.Nature communications · 2018Article
- Force generation by titin folding.Protein science : a publication of the Protein Society · 2017Article
- Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017Review
- Optical Trapping Nanometry of Hypermethylated CPG-Island DNA.Biophysical journal · 2017Article
- Kinetic Ductility and Force-Spike Resistance of Proteins from Single-Molecule Force Spectroscopy.Biophysical journal · 2016Article
- Computing Average Passive Forces in Sarcomeres in Length-Ramp Simulations.PLoS computational biology · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is a giant filamentous protein of the muscle sarcomere in which stretch induces the unfolding of its globular domains. However, the mechanisms of how domains are progressively selected for unfolding and which domains eventually unfold have for long been elusive. Based on force-clamp optical tweezers experiments we report here that, in a paradoxical violation of mechanically driven activation kinetics, neither the global domain unfolding rate, nor the folded-state lifetime distributions of full-length titin are sensitive to force. This paradox is reconciled by a gradient of mechanical stability so that domains are gradually selected for unfolding as the magnitude of the force field increases. Atomic force microscopic screening of extended titin molecules revealed that the unfolded domains are distributed homogenously along the entire length of titin, and this homogeneity is maintained with increasing overstretch. Although the unfolding of domains with progressively increasing mechanical stability makes titin a variable viscosity damper, the spatially randomized variation of domain stability ensures that the induced structural changes are not localized but are distributed along the molecule's length. Titin may thereby provide complex safety mechanims for protecting the sarcomere against structural disintegration under excessive mechanical conditions.
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