SUPRAMOLECULAR STRUCTURE OF THE MAMMALIAN LENS

最近有证据表明， 哺乳动物的晶状体显然是由于 晶状体的主要蛋白质，晶状体蛋白。一种对 这一命令的性质是获得 白内障形成的分子描述(其中这个顺序是 中断)。这项研究的主要目的是描述 牛晶状体中晶体蛋白的分子间相互作用 二元蛋白质邻近度的二维空间图的形式 两性关系。这张地图将由一个系统的系列生成 使用三种晶体蛋白级分的测量结果。这个 晶体蛋白/晶体蛋白相互作用的潜在存在 在均相晶体蛋白溶液和所有 晶体蛋白可能的二元混合物作为蛋白质的函数 集中精神。任何交互作用的功能意义 检测到的将根据观察到的发病情况进行评估 增加了在高蛋白下的光学透明度 晶状体蛋白提取物中的浓度。评选出的 要使用的实验方法是基于最小化的愿望 蛋白质表面的微扰和需要使 对异常广泛的蛋白质进行测量 浓度。在此基础上，提出了动态光照技术 散射、化学交联和荧光能量转移 用来研究晶体蛋白/晶体蛋白的相互作用。 此外，还将探讨钙和氯化钠的影响。 因为已知这些试剂对聚集的影响 晶状体蛋白。由此产生的超分子描述 透镜的相对拓扑位置 然后，晶体蛋白将作为未来的框架，在其中 研究与白内障相关的现象。

It has recently been demonstrated that the transparency of the mammalian lens is apparently due to short range order among the major proteins of the lens, the crystallins. An understanding of the nature of this order is an essential step in obtaining a molecular description of cataract formation (in which this order is disrupted). The major objective of this research is to describe intermolecular interactions between bovine lens crystallins in the form of a two dimensional spatial map of binary protein proximity relationships. This map will be generated by a systematic series of measurements employing three crystallin fractions. The potential existence of crystallin/crystallin interactions will be addressed within both homogeneous crystallin solutions and in all possible binary mixtures of crystallins as a function of protein concentration. The functional significance of any interactions detected will be evaluated based on the observation of the onset of increasing optical transparency seen at high protein concentrations in lens protein extracts. The selection of the experimental methods to be used is based on a desire to minimize perturbation of protein surfaces and a need to make measurements over an unusually wide range of protein concentrations. On this basis, the techniques of dynamic light scattering, chemical crosslinking and fluorescence energy transfer have been chosen to examine crystallin/crystallin interactions. The effect of calcium and sodium chloride will also be explored because of the known effects of these agents on the aggregation of crystallins. The resulting supra-molecular description of the lens in terms of the relative topological locations of the crystallins will then serve as a future framework within which to study cataract related phenomena.