Research Coordination Network: Protein Folding and Dynamics

职务名称：研究协调网络：蛋白质折叠和动力学这个研究协调网络的目标：蛋白质折叠联盟（RCN：PFC）是提供一个新的平台，用于建立和培养实验学家，理论家和计算生物学家之间的合作和培训，他们专注于获得分子水平的蛋白质折叠和其他动力学过程的理解。 蛋白质在自然界中无处不在，执行多种生物功能，如用防御剂填充免疫系统以对抗病毒感染，消化食物，作为创造皮肤，肌肉和头发的材料，将来自环境的信号转化为细胞反应和复制DNA。RCN：PFC将探索蛋白质采用其独特形状的分子机制，以及这些形状使其维持生命的功能过剩的动态过程。 这些现象非常复杂，需要实验和计算方法方面的专家组成的联盟来了解它们的性质。该联盟还旨在为该领域的年轻科学家提供一个新颖的互动培训和指导平台。为了实现这些目标，PFC将支持两次年度会议，一次是与主要研究者，另一次是与研究者及其学生，并支持一个网站。在许多方面，该联盟作为一个虚拟研究所，专注于研究生物学中最重要和最迷人的问题之一。蛋白质折叠联盟（Protein Folding Consortium，PFC）的目标是通过建立一个由实验学家、生物学家和生物学家组成的联盟来改变科学家对蛋白质折叠问题和蛋白质动力学的认识，并通过建立一个由实验学家、生物学家和生物学家组成的联盟来促进蛋白质折叠的研究。理论家和计算生物学家，他们的集体努力超过了单个实验室所能达到的进展。 高性能计算的进步结合新颖的采样方法和复杂实验的应用，现在使模拟和实验研究蛋白质折叠和动力学在类似的时间尺度上。 模拟为实验生成可测试的预测。实验结果可用于改进模拟方法和力场。这种模拟和实验之间的迭代协同方法，当部署在不同折叠，大小，复杂性和进化概况的蛋白质时，将允许对折叠过程进行连贯和收敛的描述。 PFC的扩展目标包括体内折叠，生物物理性质的演变，内在无序蛋白质的耦合折叠和结合，大分子机器和功能动力学。 这些新的冒险都以这样或那样的方式与蛋白质的折叠自由能表面及其受序列、历史和环境的调节有关。 该项目由生物科学理事会分子和细胞生物科学部的分子生物物理学集群联合资助;物理学部的生命系统物理学计划，以及数学和物理科学理事会化学部的生命过程化学计划。

Title: Research Coordination Network: Protein Folding and DynamicsThe objective of this Research Coordination Network: Protein Folding Consortium (RCN:PFC) is to provide a novel platform for establishing and nurturing collaborations and training between experimentalists, theorists and computational biologists who are focused on obtaining a molecular-level understanding of the folding and other dynamical processes of proteins. Proteins are ubiquitous in nature, executing biological functions as diverse as populating the immune system with defense agents against viral infections, digesting food, serving as materials to create skin, muscle and hair, converting signals from the environment into cellular responses and replicating DNA. The RCN:PFC will probe the molecular mechanisms by which proteins adopt their unique shapes and the dynamic processes by which those shapes enable their plethora of functions that maintain life. These phenomena are sufficiently complex that a consortium of experts in both experimental and computational methods is required to understand their properties. The consortium also aims to provide a novel and interactive training and mentoring platform for younger scientists in the field. To achieve these objectives, the PFC will support two annual meetings, one with the principal investigators and another with the investigators and their students, and a website. In many ways, the consortium acts as a virtual institute focused on a studying one of the most important and fascinating problems in biology. It is anticipated that accelerated progress towards a deeper understanding of the fundamental principles that govern protein folding reactions and protein dynamics will have a major impact on biochemistry, medicine and the biotechnology industry.The goal of this Protein Folding Consortium (PFC) is to transform the way that scientists think about the protein folding problem and protein dynamics by creating a consortium of experimentalists, theorists and computational biologists whose collective efforts exceed the progress attainable by individual labs. Advances in high performance computing combined with novel sampling methods and the application of sophisticated experiments now make it possible for simulations and experiments to study protein folding and dynamics on similar time scales. Simulations generate testable predictions for experiments. Results from experiments can be used to refine simulation methodologies and force fields. This iterative synergistic approach between simulation and experiment, when deployed across proteins of different folds, sizes, complexity and evolutionary profiles, will allow for a coherent and convergent description of the folding process. The expanding ambitions of the PFC encompass folding in vivo, the evolution of biophysical properties, the coupled folding and binding of intrinsically disordered proteins, macromolecular machines and functional dynamics. These new ventures are related, in one way or another, to the folding free energy surface of a protein and its modulation by sequence, history and the environment. This project is jointly funded by the Molecular Biophysics Cluster in the Division of Molecular and Cellular Biosciences in the Directorate for Biological Sciences; the Physics of Living Systems Program in the Division of Physics, and the Chemistry of Life Processes Program in the Division of Chemistry in the Directorate of Mathematical and Physical Sciences.