Understanding of cooperative actions between skeletal myosin molecules

我试图通过测量单个肌凝蛋白排列在肌凝蛋白杆细丝中产生的位移和力来捕捉单个骨骼肌凝蛋白的“真实”力学特性，这比以往单分子研究中设计的典型实验设置更自然。结果表明，单个肌凝蛋白的弹性特性是非线性的。肌凝蛋白受到拉伸时，它会变得更硬，这样它可以用很小的拉伸产生很大的力，而当它受到压缩时，它会变得更软，以减少阻力。因此，非线性弹性可能是一种巧妙的机械特性，可以在没有马达之间分子干扰的情况下有效地实现肌肉收缩。

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.