C ELEGANS THICK FILAMENT ASSEMBLIES

CELEGANS 粗丝组件

• 批准号: 6611279
• 负责人: HENRY F. EPSTEIN
• 金额: $ 13.47万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2001
• 资助国家: 美国
• 起止时间: 2001-12-01 至 2002-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6611279
• 关键词: animal tissue; biomedical resource; growth /development; musculoskeletal system

We have proposed a three-dimensional model for the structure of the backbones of thick filaments of the nematode Caenorhabditis elegans, based on electron microscopy and image analysis. In this model, the core is a tubule of seven paramyosin subfilaments, coupled by crosslinking proteins. Thick filament rigidity is a necessary element in the sliding-filament theory of muscle contraction. We have measured the rigidity displayed by these structures in electron micrographs, by the stochastic measure of persistence length. The conventional model of vertebrate thick filaments based solely upon the intertwining of myosin tails in a ropelike manner cannot explain their exceptional flexural rigidity. The coupled tubule principle may explain the rigidity observed in thick filaments and other linear structures

我们提出了一个三维模型的结构， 小杆线虫粗丝的骨干 基于电子显微镜和图像分析的秀丽隐杆线虫。 在这 模型，核心是一个小管的七副肌球蛋白亚丝，耦合 通过交联蛋白质。 粗灯丝的刚性是必要的 肌肉收缩的滑丝理论中的一个元素。 我们有 测量了这些结构在电子中显示的刚性， 显微照片，通过持久性长度的随机测量。 的 传统的脊椎动物粗丝模型仅仅基于 肌球蛋白尾部以绳状方式缠绕不能解释它们的 卓越的抗弯刚度。 偶联小管原理可以 解释在粗纤维和其他线性纤维中观察到的刚性 结构