THICK FILAMENT MYOSIN AND C-PROTEIN ARRANGEMENT

粗丝肌球蛋白和 C 蛋白排列

基本信息

批准号：
3152065
负责人：
Robert W. Kensler
金额：
$ 11.01万
依托单位：
ALLEGHENY UNIVERSITY OF HEALTH SCIENCES
依托单位国家：
美国
项目类别：
财政年份：
1982
资助国家：
美国
起止时间：
1982-01-01 至 1987-11-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/3152065
关键词：
computer graphics /printing electron microscopy fresh water environment gel electrophoresis muscle function muscle proteins myofibrils optics species difference striated muscles

项目摘要

The arrangement of myosin and accessory proteins such as C-Protein in the vertebrate striated muscle thick filament is incompletely known. Recent experiments on the structure of frog thick filaments, however, have demonstrated that the structure of vertebrate thick filaments may be amenable to analysis by a combination of electron microscopy, optical diffraction analysis, and computer image reconstruction techniques. The specific aim of the proposed research is to expand these studies of the frog thick filaments and to extend the studies to the determination and comparison of the structure of thick filaments isolated from fish, avian, and mammalian striated muscle. The major objective of these studies will be the determination of the arrangement and number of myosins per crossbridge level in these filaments and how C-protein is arranged relative to the underlying myosin. The studies to accomplish these aims will include: 1) the development of procedures fro the isolation of native thick filaments with minimal structural alteration from each of the species; 2) the use of combination of electron microscopy and optical diffraction analysis of the micrographs to assess the filament preservation; and 3) the use of computer image analysis of the filament images in the best electron micrographs to determine the rotational symmetry and arrangement of the myosin heads, and the arrangement of C-protein. These studies will provide basic scientific information about the structure of muscle, and will thus provide a better foundation for understanding how pathologic condition may affect the functioning of this tissue.

肌球蛋白和辅助蛋白（如 C 蛋白）的排列脊椎动物横纹肌的粗丝尚不完全清楚。最近的然而，对青蛙粗丝结构的实验却发现证明脊椎动物粗丝的结构可能是可以结合电子显微镜、光学显微镜进行分析衍射分析和计算机图像重建技术。这拟议研究的具体目的是扩大这些研究青蛙粗丝并将研究扩展到测定和从鱼类、鸟类中分离出的粗丝的结构比较和哺乳动物横纹肌。这些研究的主要目标将是决定每个肌球蛋白的排列和数量这些细丝中的桥水平以及 C 蛋白的相对排列方式到底层的肌球蛋白。为实现这些目标而进行的研究将包括：1）程序的开发脱离native 粗丝，每个的结构变化最小物种; 2）电子显微镜与光学相结合的使用通过显微照片的衍射分析来评估灯丝保存; 3）利用计算机图像分析灯丝最佳电子显微照片中的图像以确定旋转肌球蛋白头的对称性和排列，以及 C-蛋白。这些研究将提供有关以下方面的基本科学信息：肌肉的结构，从而为了解病理状况如何影响其功能组织。