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With substantial evidence, Hugh Huxley formally proposed the mechanism for sliding filament which is variously called swinging cross-bridge model, cross-bridge theory or cross-bridge model. [ 3 ] [ 30 ] (He himself preferred the name "swinging crossbridge model", because, as he recalled, "it [the discovery] was, after all, the 1960s". [ 2 ] )
Cross-bridge cycle. Cross-bridge cycling is a sequence of molecular events that underlies the sliding filament theory. A cross-bridge is a myosin projection, consisting of two myosin heads, that extends from the thick filaments. [1] Each myosin head has two binding sites: one for adenosine triphosphate (ATP) and another for actin.
Activation consists of phosphorylation of a serine on position 19 (Ser19) on the MLC 20 light chain, which causes a conformational change that increases the angle in the neck domain of the myosin heavy chain, [8] which corresponds to the part of the cross-bridge cycle where the myosin head is unattached to the actin filament and relocates to ...
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The muscle cells need ATP (adenosine triphosphate) as it provides energy for muscle contraction by actively transporting calcium ions into the sarcoplasmic reticulum before muscle contraction, and it is used during muscle contraction for the release of myosin heads in the sliding filament model during the cross-bridge cycle.
Two models of nuclear congression have been proposed: the sliding cross-bridge, and the plus end model. In the sliding cross-bridge model, the microtubules run antiparallel to each other for the entire distance between the two pronuclei, forming cross-links to each other, and each attaching to the opposite nucleus at the plus end. This is the ...
Specifically, it increases the rate of phosphate release from myosin by stabilizing the pre-powerstroke and the phosphate release states, [8] thereby accelerating the rate-determining step of the cross-bridge cycle, which is the transition of the actin-myosin complex from the weakly bound to the strongly bound state.
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