COMPUTATIONAL STUDY OF MOTOR PROTEINS: FREE ENERGY OF CONFORMATIONAL STATES OF

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 关键词：运动蛋白；肌肉收缩；自由能源；构象状态； ATP水解 肌球蛋白头构象状态的平均力势 具有不同结合核苷酸配体的蛋白质 S1 将使用以下方法计算 伞采样技术。结果数据将与 随机动力学模型提供对 生物细胞中的工作产生机制。这样的相关性 了解运动蛋白复合物的运作以设计 纳米级的人造分子马达也将受到研究。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Keywords: Motor protein; muscle contraction; free energy; conformational states; ATP hydrolysis The potentials of mean force of the conformational states of myosin head protein S1 with different bound nucleotide ligands will be calculated using the umbrella sampling technique. The resulting data will be combined with stochastic dynamical models to provide a quantitative understanding of the mechanism of work production in biological cells. Relevance of such an understanding of the operation of motor protein complexes to the design of artificial molecular motors in the nano-scale will also be examined.