MECHANISM OF KINESIN ATPASE

描述。这项研究的长期目标是提供更好的 对细胞内细胞器沿线运动机制的认识 微管的这种运动在FAST过程中起着特殊的作用 神经细胞中的轴突运输。这一过程提供了一种方法 将新合成的物质从它们的合成部位转移到 神经细胞体与轴突末端的突触相连。激动素有 广泛存在于多种高等真核生物中，并存在于大多数细胞中 类型，而不仅仅是神经元。在这些其他类型的细胞中，激动素很可能是 负责部分类别膜泡的相关转运 朝向细胞的外围。与之相关的其他蛋白质 Kinesin负责沿纺锤体微管的部分运动 在细胞分裂过程中。在拟议研究中开发的信息还将 也适用于这些其他重要的马达蛋白。 驱动动蛋白运动的能量是由水解物提供的。 三磷酸腺苷(ATP)的含量。拟议工作的一个主要目标是 重点确定了ATP水解酶的详细作用机理 关于水解的化学能变化是如何与物理耦合的 沿着微管运动的过程。因为运动的结果是 从酶构象的变化来看，同样重要的是 了解酶的结构以及它在催化过程中的变化。 一种正在进行的方法是对 激动素。最新进展表明，激动素在体内折叠成一个 被抑制的形式，需要展开才能成为活动的马达。这个 折叠是由两端的区域相互作用产生的 蛋白质与折叠过程调控及影响因素的研究 对它的影响将会被执行。将广泛使用稳定的和 研究了单次周转的动力学机制。这些 酶学研究将与运动蛋白的运动性研究相结合。 能够生产的。远程目标是能够对物理模型进行建模 基于其溶液生化机理的激动素的性质，

DESCRIPTION. The long range goal of this research is to provide a better understanding of the mechanism of movement of intracellular organelles along microtubules, Such movement plays a special role in the process of fast axonal transport in nerve cells. This process provides one means for the movement of newly synthesized material from their site of synthesis in the body of a nerve cell to the synapse at the end of the axon. Kinesin has been found in a wide range of higher eukaryotes and are present in most cell types, not just neurons. In these other cell types, kinesin is likely responsible for the related transport of some classes of membrane vesicle towards the periphery of the cell. Other proteins that are related to kinesin are responsible for part of the movement along spindle microtubules during cell division. Information developed in the proposed study will also be applicable to these other important motor proteins. The energy that drives the movement of kinesin is provided by the hydrolysis of adenosine triphosphate (ATP). A principal aim of the proposed work is to determine the detailed enzymatic mechanism of ATP hydrolysis with emphasis on how the chemical energy change of hydrolysis is coupled to the physical generation of movement along a microtubule. Because the movement results from changes in the conformation of the enzyme, it is also important to understand the structure of the enzyme and how it changes during catalysis. One ongoing approach is characterization of the individual domain of kinesin. Recent progress indicates that kinesin is folded in vivo into an inhibited form that needs to unfold before it can be an active motor. The folding is produced by the interaction of regions in the two ends of the protein and the study of the regulation of the folding process and factors influencing it will be performed. Extensive use will be made of steady and single turnover kinetics in the investigation of the mechanism. These enzymatic studies will be coupled with study of the motility that kinesin is able to produce. A long range goal is to be able to model the physical properties of kinesin based on its solution biochemical mechanism,