Understanding of cooperative actions between skeletal myosin molecules

我试图捕捉“真正的”机械性能的单个骨骼肌肌球蛋白通过测量的位移和力所产生的单个肌球蛋白排列在肌球蛋白杆共丝，这是更自然的环境比典型的实验装置设计在以前的单分子研究。结果发现，单个肌球蛋白的弹性性质是非线性的。当肌球蛋白被拉伸时，它变得更硬，以便它可以用很小的拉伸产生很大的力，而当它被压缩时，它变得更软，以减少阻力。因此，非线性弹性可能是一种巧妙的机械特性，可以有效地实现肌肉收缩，而无需电机之间的分子干扰。

I have tried to capture the "true" mechanical properties of single skeletal myosins by measuring the displacement and force generated by single myosins arranged in myosin-rod cofilaments, which is more natural environment than the typical experimental setup designed in the previous single molecule studies. It was found that the elastic properties of single myosins is non-linear. When a myosin is stretched, it becomes stiffer so that it can generate a large amount of force with a small stretching, while it becomes much softer to reduce the resistance force when it is compressed. Therefore, the non-linear elasticity may be an ingenious mechanical property to achieve muscle contractions efficiently without the molecular interference between motors.