ArticleBiophysical journal2005
Stepwise length changes in single invertebrate thick filaments.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Emergent spatiotemporal dynamics of the actomyosin network in the presence of chemical gradients.Integrative biology : quantitative biosciences from nano to macro · 2019Article
- Emergent mechanics of actomyosin drive punctuated contractions and shape network morphology in the cell cortex.PLoS computational biology · 2018Article
- Contraction-Induced Changes in Hydrogen Bonding of Muscle Hydration Water.The journal of physical chemistry letters · 2014Article
- Rotational model for actin filament alignment by myosin.Journal of theoretical biology · 2012Article
- Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Journal of biomedicine & biotechnology · 2010Review
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Authors and funding
3 authors.
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Abstract
Previous experiments on thick filaments of the anterior byssus retractor muscle of Mytilus and the telson-levator muscle of Limulus polyphemus have shown large, reversible length changes up to 23% and 66% of initial length, respectively, within the physiological tension range. Using nanofabricated cantilevers and newly developed high-resolution detection methods, we investigated the dynamics of isolated Mytilus anterior byssus retractor muscle thick filaments. Single thick filaments were suspended between the tips of two microbeams oriented perpendicular to the filament axis: a deflectable cantilever and a stationary beam. Axial stress was applied by translating the base of the deflectable nanolever away from the stationary beam, which bent the nanolever. Tips of flexible nanolevers and stationary beam were imaged onto a photodiode array to track their positions. Filament shortening and lengthening traces, obtained immediately after the motor had imposed stress on the filament, showed steps and pauses. Step sizes were 2.7 nm and integer multiples thereof. Steps of this same size paradigm have been seen both during contraction of single sarcomeres and during active interaction between single isolated actin and myosin filaments, raising the question whether all of these phenomena might be related.
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