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

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 关键词：运动蛋白；肌肉收缩；自由能；构象状态；三磷酸腺苷水解酶 肌球蛋白头部构象状态的平均作用力势 具有不同结合核苷酸配体的蛋白质S1将使用 伞状抽样技术。生成的数据将与 随机动力学模型，以提供对 生物细胞中做功产生的机制。此类产品的相关性 对运动蛋白复合体运作的理解 还将研究纳米尺度的人造分子马达。

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.