ArticleProtein science : a publication of the Protein Society2017
Force generation by titin folding.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- Shining Light in Mechanobiology: Optical Tweezers, Scissors, and Beyond.ACS photonics · 2024Review
- Nanosurgical Manipulation of Titin and Its M-Complex.Nanomaterials (Basel, Switzerland) · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Tools for studying and modulating (cardiac muscle) cell mechanics and mechanosensing across the scales.Biophysical reviews · 2021Review
- Model systems for optical trapping: the physical basis and biological applications.Biophysical reviews · 2021Review
- Mechanisms ofJournal of cardiovascular development and disease · 2021Review
- Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.International journal of molecular sciences · 2021Article
- The structural role of osteocalcin in bone biomechanics and its alteration in Type-2 Diabetes.Scientific reports · 2020Article
- Single-Cell Elasticity Measurement with an Optically Actuated Microrobot.Micromachines · 2020Article
- Posttranslational modifications of titin from cardiac muscle: how, where, and what for?The FEBS journal · 2019Review
- Stretch your heart-but not too far: The role of titin mutations in dilated cardiomyopathy.The Journal of thoracic and cardiovascular surgery · 2018Review
- The Work of Titin Protein Folding as a Major Driver in Muscle Contraction.Annual review of physiology · 2018Review
- ATP prevents Woronin bodies from sealing septal pores in unwounded cells of the fungus Zymoseptoria tritici.Cellular microbiology · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is a giant protein that provides elasticity to muscle. As the sarcomere is stretched, titin extends hierarchically according to the mechanics of its segments. Whether titin's globular domains unfold during this process and how such unfolded domains might contribute to muscle contractility are strongly debated. To explore the force-dependent folding mechanisms, here we manipulated skeletal-muscle titin molecules with high-resolution optical tweezers. In force-clamp mode, after quenching the force (<10 pN), extension fluctuated without resolvable discrete events. In position-clamp experiments, the time-dependent force trace contained rapid fluctuations and a gradual increase of average force, indicating that titin can develop force via dynamic transitions between its structural states en route to the native conformation. In 4 M urea, which destabilizes H-bonds hence the consolidated native domain structure, the net force increase disappeared but the fluctuations persisted. Thus, whereas net force generation is caused by the ensemble folding of the elastically-coupled domains, force fluctuations arise due to a dynamic equilibrium between unfolded and molten-globule states. Monte-Carlo simulations incorporating a compact molten-globule intermediate in the folding landscape recovered all features of our nanomechanics results. The ensemble molten-globule dynamics delivers significant added contractility that may assist sarcomere mechanics, and it may reduce the dissipative energy loss associated with titin unfolding/refolding during muscle contraction/relaxation cycles.
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