Chemical and Mechanical Interactions in Microtubules

[9710354]这个提议带来了定量的，工程的角度来研究微管（MTs）的化学和力学特性，在大多数动物细胞质中发现的管状蛋白细丝。提出的研究的三个目的是：在蝾螈肺细胞和成纤维细胞的前沿MTs动态的数字图像分析。本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，并研究MT组装和拆卸的热力学。假设能量以应变的形式储存在MT晶格中。将使用特异性MT相关蛋白（MAPs）来破坏微管，并通过量热法测量能量释放。将研究MT与MAP在应变上的结合关系。MT切断酶的活性，katanin，将被测量为应变和未应变的微管。卡他宁可能是体内MT转换的关键调节因子。＊＊＊

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. ***