Abstract
Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement. Furthermore, they have also demonstrated that in response to strain in the backward direction a detached myosin head preferentially attaches to the forward direction due to an accelerated transition from a weak binding to strong binding state. Because they are consistent with the original Huxley model for muscle contraction, we have built a model that describes macroscopic muscle characteristics based on these single molecule results.
Highlights
Drs Michael and Kate Barany were an excellent team in the world of muscle research
Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement
Single molecule measurements have suggested that muscle operates by the Brownian search-and-catch mechanism, which assumes myosin heads undergo Brownian motion back and forth along the actin filament in the presence of ATP while they attach and detach rapidly (Dunn and Spudich 2007; Shiroguchi and Kinosita 2007; Iwaki et al 2006)
Summary
Drs Michael and Kate Barany were an excellent team in the world of muscle research. It is a testament to their work that their names will be long remembered.More than 50 years ago, using contemporary structural and physiological data, A.F. Abstract Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement. They have demonstrated that in response to strain in the backward direction a detached myosin head preferentially attaches to the forward direction due to an accelerated transition from a weak binding to strong binding state.
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