MEMBRANE PROTEIN STRUCTURAL DYNAMICS CONSORTIUM

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。 膜蛋白在物质和信息的交换中起着至关重要的作用 活细胞和它们的环境之间，能量的流动和使用， 在许多信号通路中。因此，它们参与几乎所有的细胞 对细胞和生物体的生存、发育和健康至关重要的过程。 实验结构生物学的最新进展，特别是在过去十年中， 积累了丰富的膜蛋白结构信息，揭示了关键的 元素的功能。然而，它很快就变得明显，静态结构是 不足以充分表征膜蛋白的功能，为了充分 了解它们的机制，动力学描述是必要的。构象和 相互作用动力学对膜的功能行为有很大的影响 蛋白质，因为它是结构和动力学之间的相互作用，最终定义了一个 生物系统的功能机制。了解这些基本的 现象影响膜蛋白功能的方式是理解 复杂的网络信号和能量转导机制涉及正常 细胞功能及其病理学。有着悠久的传统，在研究广泛的 与世界领先的实验小组合作， 资源与一个恒星研究小组的共同努力， 目标是应用最先进的生物物理方法， 膜蛋白的结构动力学达到了前所未有的水平。由于这种 膜蛋白结构动力学联合会（MPSDC） (http：memprotein.org）的“胶水赠款”， 2010年，NIH国家普通医学科学研究所。该联盟旨在 在解决膜蛋白的基本动力学现象，通过一个 高度互动、紧密结合和多学科努力， 在各种生物学中，结构、动态和功能之间的关系 膜蛋白MPSDC围绕多学科项目组织 由来自五个不同国家的14个机构的调查人员组成的小组。这些 团队研究与膜蛋白功能相关的主要机制问题 在两个主要领域：信号传导中的能量转导（离子通道和受体） 和能量相互转换（输送机和泵）。最终，我们 目标是解码控制蛋白质运动的一般机械原理 及其相关的波动动力学通过解剖和分析分子 以及这些功能的动力基础， 以及利用这些信息来设计改变和新颖的活动， 膜蛋白框架，以合理地进化新的功能。

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. Membrane proteins play an essential role in the exchange of material and information between living cells and their environment, the flow and use of energy, and in numerous signaling pathways. As such, they participate in almost all cellular processes fundamental to the living, development, and well being of cells and organisms. Recent advances in experimental structural biology, specially over the last decade, have accumulated a wealth of structural information on membrane proteins, revealing key elements for their function. However, it became soon evident that static structures are not sufficient to fully characterize the function of membrane proteins, and in order to fully understand their mechanism, a dynamical description is necessary. Conformational and interaction dynamics have a large impact on the functional behavior of membrane proteins, for it is the interplay between structure and dynamics that ultimately defines a biological system's functional mechanism. Knowledge of how these fundamental phenomena influence the way membrane proteins function is required to understand the complex web of signaling and energy transduction mechanisms involved both in normal cellular function and their pathologies. Having a long tradition in studying a wide range of membrane proteins in collaboration with leading experimental groups in the world, the Resource joined efforts with a stellar group of researchers with the common goal of applying state of the art biophysical methodologies to investigate at an unprecedented level the structural dynamics of membrane proteins. As a result of this joint effort, the "Membrane Protein Structural Dynamics Consortium (MPSDC)" (http://memprotein.org) was formed and funded through a "Glue Grant" by the NIH National Institute of General Medical Sciences in 2010. The consortium aims at addressing fundamental dynamical phenomena in membrane proteins through a highly interactive, tightly integrated and multidisciplinary effort focused on elucidating the relationship between structure, dynamics and function in a variety of membrane proteins. The MPSDC is organized around multidisciplinary project teams formed by investigators from 14 institutions in five different countries. These teams study major mechanistic questions associated with membrane protein function in two major areas: energy transduction in signaling (ion channels and receptors) and energy inter-conversion (transporters and pumps). Ultimately, our goal is to decode the general mechanistic principles that govern protein movement and its associated fluctuation dynamics by dissecting and analyzing the molecular and dynamical bases of these functions at an unprecedented and quantitative level, as well as exploiting this information to engineer altered and novel activities into membrane protein frameworks to rationally evolve new functions.