CAPTURING LARGE-SCALE STRUCTURAL TRANSITIONS IN MEMBRANE TRANSPORTERS AT ATOMIC

捕获原子膜转运蛋白的大规模结构转变

• 批准号: 8364328
• 负责人: Emad Tajkhorshid
• 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/8364328
• 关键词: Automobile Driving; Binding; Biomedical Research; Cells; Coupling; Event; Funding; Grant; High Performance Computing; Life; Membrane Transport Proteins; Molecular Machines; National Center for Research Resources; Nature; Principal Investigator; Proteins; Research; Research Infrastructure; Resources; Source; Time; United States National Institutes of Health; cost; simulation

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. We request allocation on Anton for extended MD simulations that will investigate several membrane transporters representing major energy-coupling mechanisms of transport in living cells. The proposed studies will characterize the nature and magnitude of protein conformational changes induced by binding/unbinding of the substrate and the driving energy-coupling events on a microsecond time scale, and reveal structurally unknown states of the transporters. The results will bring an unprecedented time scale to the dynamical description of these slow molecular machines for the first time, and given the experimental inaccessibility of such information, will revolutionize our mechanistic view of their function.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 我们要求在安东（Anton）分配扩展的MD模拟，这些模拟将研究几个代表活细胞中运输主要能量偶联机制的膜转运蛋白。拟议的研究将表征蛋白质构象变化的性质和大小，这是通过微秒时间尺度上底物和驱动能耦合事件引起的蛋白质构象变化，并揭示了运输蛋白的结构未知状态。 结果将首次为这些慢分子机器的动态描述带来前所未有的时间尺度，并且鉴于此类信息的实验性无法获取性，将彻底改变我们对其功能的机械观点。