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Actin molecules repeat every 2.75 nm along the thin filament.
This replacement did not significantly change thin filament stoichiometry.
Nebulin, a vertebrate skeletal muscle actin binding protein, plays an important role in thin filament architecture.
Instead, myosin-binding must drive tropomyosin toward the open-state to activate the thin filament.
Cardiac troponin I (cTnI) functions as the molecular switch of the thin filament.
Striated muscles are regulated by Ca2+via the thin filament proteins troponin (Tn) and tropomyosin (Tm).
Once calcium is bound, transduction involves changes in protein interactions along the thin filament.
It involves the placement of a thin filament in a hot gas stream.
To facilitate this undertaking we assumed that specific CM mutants could be categorized as Ca2+ activating (thin filament activator) or Ca2+deactivating (thin filament deactivator) archetypes.
Myosin attachments were quantified everywhere along the thin filament including troponin.
CM sarcomeric proteins can directly cause thin filament deactivation [52] [55].
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