2012 Intrinsically Disordered Proteins Gordon Research Conference

描述（由申请人提供）：第二届内含子紊乱蛋白质（IDP）戈登研究会议将于2012年7月8日至7月13日在Mt.美国佛蒙特州西多佛的雪场。这次会议的共同主席是美国圣路易斯华盛顿大学的Rohit Pappu博士和比利时Vrije Universiteit Universel的Peter Tompa博士。 长期以来的观点是，蛋白质必须形成有序的三维结构，以实现其适当的生物功能。这一观点受到了大约30%的真核生物蛋白质不能自主折叠的观察结果的挑战，它们不能折叠是功能所必需的。这些蛋白质被称为内在无序蛋白质或IDP，涉及多种功能，包括基本过程，如转录调节、信号转导、蛋白质运输、蛋白质稳态和质量控制。 大多数生物功能都是基于分子识别，复杂的网络是围绕一系列相互关联的蛋白质-蛋白质和蛋白质-核酸界面组织起来的。传统观点认为，分子识别 是通过形状互补性和蛋白质与其结合伴侣之间的特异性相互作用的组合来实现的。设想形状的小规模变化以实现高度特异性的复合物。IDP为分子识别增加了一个全新的维度，因为它需要大规模的构象变化来实现结合。它还提出了一个具有挑战性的问题，即在没有精确的预组织形状互补性的情况下，如何实现特定的识别。然而，IDP在自然界中普遍存在，并形成了一系列复杂生物功能的基础，包括超越分子识别的新功能，IDP在自组装和熵机器中发挥作用。 越来越多的人认识到IDPs在复杂的生物学功能中的作用，这使得这是一个合适的时机，将该领域的科学家聚集在一起，以确定重要的问题，评估目前的进展，并绘制路线，以快速和有意义的进展在构象异质性及其在蛋白质功能中的作用的研究。与NIH特别相关的一点是，国内流离失所者与许多人类疾病，如神经退行性疾病和癌症有关的比例过高。从这个角度来看，2012年戈登会议的内在无序蛋白（IDP）正在形成一个令人兴奋的和重要的会议。 这次会议将提供一个及时的机会，使专家和年轻科学家聚集在一起，评估进展情况，并为国内流离失所者在基础生物学中的作用和确定国内流离失所者相关疾病（如神经退行性疾病和癌症）的新治疗靶点制定未来发展方向。该计划的特点是在IDP领域的研究前沿的杰出和多样化的科学家群体。会议将围绕七个主题会议组织，重点是转录调控，信号通路和模块，IDP阶段行为和分子识别，研究IDP的新兴技术，IDP质量控制和稳态，受监管的自组装和错误组装的IDP，以及IDP的目标，贩运和处理。会议将以两场主旨会议结束。传统上用于研究蛋白质结构和结构-功能关系的工具通常不适用于IDP的研究，因为它们潜在的构象异质性。需要新的进展，IDP戈登会议将展示最先进的生物物理方法的发展，理论和计算的进步，以及与分子生物学新工具的协同作用，用于研究IDP并对其体内功能进行定量分析。 将组织海报会议，鼓励青年科学家积极参与。组织者安排了博士后和研究生根据他们的海报展示竞争多达七个奖项，这些奖项将由IDP领域的领导者评判。本次会议的新地点风景优美，方便，并有望成为会议期间众多信息讨论的绝佳场所。与R13资金申请相关的一个主要目标是为年轻科学家参加戈登研究会议提供支持。在选择通过NIH基金获得支持的对象时，组织者将特别注意吸引属于代表性不足的少数群体的女性年轻科学家的必要性。

DESCRIPTION (provided by applicant): The 2nd Intrinsically Disordered Proteins (IDP) Gordon Research Conference will be held between July 08 and July 13, 2012, at the Mt. Snow Resort in West Dover, Vermont, USA. The Co-chairs for this conference are Dr. Rohit Pappu from Washington University in St. Louis, USA and Dr. Peter Tompa from Vrije Universiteit Brussel in Belgium. The long-held view has been that proteins have to form ordered three-dimensional structures in order to achieve their proper biological functions. This view has been challenged by the observation that roughly 30% of eukaryotic proteins fail to fold autonomously and their inability to fold is required for function. Such proteins, referred to as intrinsically disordered proteins or IDPs are implicated in a wide variety of functions that include fundamental processes such as transcriptional regulation, signal transduction, protein trafficking, protein homeostasis and quality control. Most biological functions are based on molecular recognition and complex networks are organized around a series of inter-related protein-protein and protein-nucleic acid interfaces. In the traditional view, molecular recognition is achieved through a combination of shape complementarity and specific interactions between a protein and its binding partner. Small-scale changes in shape are envisaged to achieve highly specific complexes. IDPs add an entirely new dimension to molecular recognition because it requires large- scale conformational changes to achieve binding. It also raises the challenging question of how specific recognition can be achieved in the absence of precise pre-organized shape complementarity. And yet, IDPs are ubiquitous in nature and form the basis for a range of complex biological functions including novel functions that go beyond molecular recognition whereby IDPs play roles in self-assembly and as entropic machines. The growing recognition of the role of IDPs in complex biological functions makes this an opportune time to bring together scientists in the field to identify the important questions, take stock of current progress, and chart the course for rapid and meaningful progress in the study of conformational heterogeneity and its role in protein function. A point of special relevance to NIH is that IDPs are overrepresented in association with numerous human diseases such as neurodegenerative diseases and cancer. Viewed in this light of this, the 2012 Gordon Conference on Intrinsically Disordered Proteins (IDPs) is shaping up to be an exciting and important meeting. The conference will provide a timely opportunity to bring experts and young scientists together to take stock of progress and chart the course for future developments with regards to the role of IDPs in basic biology and identifying novel therapeutic targets in IDP-associated diseases such as neurodegenerative disorders and cancers. The program features an outstanding and diverse group of scientists at the forefront of research in the IDP field. The meeting will be organized around seven thematic sessions focusing on Transcriptional regulation, Signaling pathways & modules, IDP phase behavior and Molecular recognition, Emerging Technologies for Studying IDPs, IDP quality control and homeostasis, Regulated self-assembly and mis- assembly of IDPs, and IDP targeting, trafficking and processing. The meeting will be bookended by two keynote sessions. The tools traditionally used for studying protein structures and structure-function relationships are generally unsuitable in studies of IDPs because of their underlying conformational heterogeneity. Novel advances are needed and the IDP Gordon Conference will showcase the development of state-of-the art biophysical methods, advances in theory and computation, and the synergy with novel tools from molecular biology for studying IDPs and developing a quantitative perspective on their functions in vivo. Poster sessions will be organized to encourage active participation from young scientists. The organizers have arranged for postdocs and graduate students to compete for up to seven awards based on their poster presentations, which will be judged by leaders in the IDP field. The new location for this conference is scenic, convenient, and promises to be an excellent setting for numerous information discussions during the conference. A major goal associated with this request for R13 funding is to provide support for young scientists to participate in the Gordon Research Conference. In choosing the recipients for support through NIH funds, the organizers will pay special attention to the need for drawing young scientists who are women and belong to under-represented minority groups.