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Cross bridge detachment is unaffected by fatigue whereas cross bridge attachment is reduced during fatigue [ 16].
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Compared to cTnI WT), both truncations displayed greater Ca2+-sensitivity and faster cross-bridge attachment rates at both SLs.
If S2 swings azimuthally during cross-bridge attachment so that it becomes angled with respect to the filament axis when force is initiated down the filament axis, that force will have both an azimuthal component (a torque) as well an axial component.
In the three-state model of thin filament regulation two activating ligands Ca2+ and strong cross-bridge attachment cause the regulatory proteins to dynamically transition between blocked, closed and open positions thereby orchestrating the cyclical bouts of diastole and systole in the beating heart.
In this way the cross-bridge attachment (power stroke) and detachment events of myosin to actin was followed.
This means that any sterically feasible cross-bridge attachment is faster under these conditions than during isometric contraction.
Such behavior may form the basis for an apparent velocity dependence of the cross-bridge attachment rate.
Their approach differs from ours and Bell's in that the [Ca2+] was kept constant and thin-filament kinetics were induced by changing cross-bridge attachment via mechanical perturbation.
In contrast, in the stopped-flow experiments, relaxation is likely initiated from very low levels of cross-bridge attachment because of the unloaded contraction of myofibrils preceding the Ca2+ removal.
The focus of previous experimental studies of actomyosin at the single-molecule level was mainly the cross-bridge attachment (power stroke) and detachment events of myosin to actin [9 14].
When cross-bridge attachment was rapidly lowered by suddenly turning from isometric to unloaded shortening, fluorescence changed much faster, monoexponentially, with rate constants increasing from ∼10 15 s−1 at partial Ca2+ activation to 50 80 s−1 at full Ca2+ activation.
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