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- W65697497 abstract "In isolated titin molecules, length changes may occur in discrete steps (Tskhovrebova et al., 1997; Rief et al., 1997). The extent to which such steps are preserved in the intact muscle-filament lattice has remained unclear. We carried out experiments on single isolated insect-flight-muscle myofibrils in which thin filaments had been functionally removed either by stretch beyond overlap or by a rigor-stretch protocol, leaving the connecting (titin) filaments as the sole length-absorbing agent. The myofibril was released or stretched by a motor in ramp-like fashion. The time course of length change in the single sarcomere was stepwise. The same was true for half-sarcomere lengths. The presence of steps at the sarcomere level implies that parallel filaments step synchronously, with high cooperativity. Step sizes showed a consistent distribution: The smallest size was approximately 2.3 nm, and others were integer multiples of that value. Similar results were found for stretch and release. To our knowledge, the approximately 2.3-nm step quantum is the smallest consistent biomechanical event ever demonstrated. This quantum is an order of magnitude smaller than anticipated from the folding/unfolding of a complete Ig- or fibronectin-like domain, and may imply that folding occurs in sub-domain increments. The 2.3-nm incremental length change corresponds to a single turn of the domains' beta sheet." @default.
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- W65697497 date "2000-01-01" @default.
- W65697497 modified "2023-09-28" @default.
- W65697497 title "Intact Connecting Filaments Change Length in 2.3-nm Quanta" @default.
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- W65697497 doi "https://doi.org/10.1007/978-1-4615-4267-4_18" @default.
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