Chemical and Mechanical Interactions in Microtubules

微管中的化学和机械相互作用

• 批准号: 9710354
• 负责人: David Odde
• 金额: $ 9.02万
• 依托单位: Michigan Technological University
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-08-15 至 1999-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9710354&HistoricalAwards=false
• 关键词: Chemical; Mechanical; Interactions; Microtubules

9710354 Odde This proposal brings a quantitative, engineering perspective to the study of the chemical and mechanical properties of microtubules (MTs), tubular protein filaments found in most animal cellular cytoplasm. The three aims of the proposed study are: The digital image analysis of the dynamics of MTs at the leading edge of newt lung cells and fibroblasts. This study will quantitatively measure the strain within the cell by direct observation of the dynamics and bending of the MTs. The thermodynamics of MT assembly and disassembly will be studied. The hypothesis is that energy is stored as strain in the MT lattice. Specific MT associated proteins (MAPs) will be used to disrupt the microtubules and the energy release will be measured by calorimetry. The relationship of MT to MAP binding on the strain will be studied. The activity of the MT severing enzyme, katanin, will be measured for both strained and unstrained microtubules. Katanin may be a key regulator of MT turnover in-vivo. ***

9710354 Odde 该提案为微管 (MT) 的化学和机械特性的研究带来了定量的工程视角，微管是大多数动物细胞质中发现的管状蛋白丝。 本研究的三个目标是： 对蝾螈肺细胞和成纤维细胞前沿的 MT 动态进行数字图像分析。 这项研究将通过直接观察 MT 的动力学和弯曲来定量测量细胞内的应变。 将研究MT组装和拆卸的热力学。 假设能量以应变形式存储在 MT 晶格中。 特定的 MT 相关蛋白 (MAP) 将用于破坏微管，并通过量热法测量能量释放。 将研究 MT 与菌株上 MAP 结合的关系。 将测量拉紧和未拉紧微管的 MT 切断酶剑蛋白的活性。 Katanin 可能是 MT 体内周转的关键调节因子。 ***