Physical-Chemical Basis of the Contractile Mechanism

力是肌肉收缩时肌球蛋白分子牵引产生的 肌动蛋白丝在缩短过程中。这个过程的细节有 由于快速和不同步， 相对滑动过程中发生的许多变化的性质 的细丝。我们的工作重点是结构性变化 被认为发生在肌球蛋白的头部区域 在这种互动中。分子生物学的引入 近年来的技术使我们能够修改 肌球蛋白的多肽结构，以这种方式，报告基团 可以更容易地引入分子中。这些基团可以 可以是用于光谱研究的荧光探针， 用于电子显微镜直接观察的探针。这些 这些方法应该提供关于肌球蛋白动力学的新信息 在ATP水解和肌动蛋白结合过程中的过桥运动， 在肌肉运动过程中， 收缩。

Force is developed in muscle contraction by myosin molecule pulling actin filaments during shortening. The details of this process have been difficult to establish because of the rapid and unsynchronized nature of the many changes taking place during the relative sliding of the filaments. Our work is focused on the structural changes that are thought to be occurring in the head region of myosin during this interaction. The introduction of molecular biological techniques in recent years has permitted us to modify the polypeptide structure of myosin in such a way that reporter groups can be more readily introduced into the molecule. These groups can be fluorescent probes for spectroscopic studies, or electron dense probes for direct visualization by electron microscopy. These methods should provide new information about the dynamics of myosin crossbridge movement during ATP hydrolysis and actin binding, both in individual molecules and in muscle fibers during muscle contraction.