STEPPING MECHANISM OF MOLECULAR MOTOR PROTEIN MYOSIN

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 马达蛋白存在于几乎所有真核细胞中。它们将化学能从 三磷酸腺苷水解为机械功，为肌肉收缩和定向运动提供动力 沿着细胞骨架的足迹。多年来，马达蛋白质的结构基础 通过解决不同区域的X射线和低温电磁结构，已经建立了工作 几种马达蛋白的结合。仍然缺少的是将不同的 马达蛋白催化循环的状态。通过与单分子专家合作 来自UIUC这里的Selvin实验室的技术，我们希望获得对 运动蛋白(http://www.ks.uiuc.edu/Research/motor).)的步进机制

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Motor proteins are found in almost all eukaryotic cells. They convert chemical energy from ATP hydrolysis to mechanical work that power muscle contraction and directional movement along cytoskeletal tracks. Over the years, the structural basis of how the motor proteins work has been established by solving the X-ray and cryo- EM structure for different domains of several motor proteins. What remains missing is the dynamic process connecting different states of motor protein's catalytic cycle. By teaming up with experts of single-molecule techniques from the Selvin lab here at UIUC, we hope to gain a molecular understanding of the stepping mechanism of motor protein (http://www.ks.uiuc.edu/Research/motor).