THE ATOMISTIC SCALE KINESIN MECHANISM ELUCIDATED ON THE EXPERIMENTAL TIME SCALE

实验时间尺度上阐明的原子尺度驱动蛋白机制

• 批准号: 8364330
• 负责人: Wonmuk Hwang
• 金额: $ 0.11万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-15 至 2013-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364330
• 关键词: Biomedical Research; Biophysics; Funding; Grant; High Performance Computing; Kinesin; Length; Mechanics; Motor; National Center for Research Resources; Principal Investigator; Proteins; Research; Research Infrastructure; Resources; Source; Time; United States National Institutes of Health; cell motility; cost; research study; response; simulation; single molecule

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. Understanding the mechanism of kinesin, the smallest known processive motor protein, is a fundamental problem in biophysics. Single molecule experiments suggest that the structural changes responsible for kinesin's dynamic motility occur within tens of microseconds. Consequently, atomic MD simulations of comparable length, which can be performed on Anton, are proposed to obtain an unbiased description of the atomic mechanism. Further, for direct comparison with experiment, we will determine the response to a fluctuating external load during the force-generating substep. The results will have general implications for understanding the mechanical interactions of many translocating motor proteins.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 驱动蛋白是目前已知的最小的运动蛋白，了解其运动机制是生物物理学中的一个基本问题。单分子实验表明，驱动蛋白的动态运动性的结构变化发生在几十微秒内。 因此，原子MD模拟的可比长度，这可以在安东，提出了获得一个公正的描述原子机制。 此外，为了与实验直接比较，我们将确定在力产生子步骤期间对波动外部载荷的响应。 这些结果将对理解许多易位马达蛋白的机械相互作用具有普遍意义。