STRUCTURE-FUNCTION RELATIONS IN MYOSIN

需要有关肌动蛋白和肌球蛋白之间的界面的详细信息 为了更好地了解肌动蛋白-肌球蛋白的各个方面 肌肉收缩的跨桥循环背后的相互作用。我们 还需要肌球蛋白重链和肌球蛋白重链之间相互作用的信息 轻链，了解轻链的功能和地形 肌球蛋白S-1。鉴于所谓的铰链的重要性 肌球蛋白交叉桥在体内运动的区域，关于 杆的不同部分的构形是理想的。因此， 申请将集中于以下具体目标：1)。鉴定 使用多个双官能团交联剂的界面区域 各种条件。2)。完成对 肌球蛋白杆的初级结构。3)。关于构象问题的探讨 通过检测巯基对肌球蛋白棒不同部分的作用 二硫键的形成和这些区域对蛋白质降解的敏感性 各种条件下的酶。4)。分子中轻链的局域化 通过交联化实验与重链的关系。5)。交联化 LMM的研究和相互作用区的识别 获取与细丝形成相关的信息。关于…的知识 正常肌肉将作为参考，并最终可能被证明在 肌肉组织病的诊断、治疗和预防 和心血管系统。

Detailed information about the interface between actin and myosin is needed for a better understanding of various aspects of the actin-myosin interaction underlying the crossbridge cycle of muscle contraction. We also need information on the interaction between myosin heavy chains and light chains to understand the function of light chains and the topography of myosin S-1. In view of the importance attributed to the so-called hinge regions in the in vivo motion of myosin cross-bridges, information on the conformation of various portion of the rod is desirable. Thus the application will focus on the following specific aims: 1). Identification of the interface regions using a number of bifunctional crosslinkers under a variety of conditions. 2). Completion of the determination of the primary structure of myosin rod. 3). Exploration of the conformation of different portions of myosin rod by examining the ability of sulfhydryls to form disulfide bonds and the susceptibility of these regions to proteolytic enzymes under various conditions. 4). Localization of light chains in relation to heavy chains by crosslinkling experiments. 5). Crosslinking studies of LMM and identification of the interaction regions with a view to obtaining information relevant to filament formation. The knowledge of normal muscle will serve as a reference and may eventually prove useful in the diagnosis, treatment, and prevention of disease involving muscle tissue and the cardiovascular system.