2007 Electron Distribution & Chemical Bonding Gordon Research Conference

描述：戈登电子分布和化学键研究会议（GRC）。动力学和密度。Mount Holyoke College, South Hadley， MA， USA， 2007年7月1-6日。该GRC传统上旨在提供一个论坛，讨论在测量和计算与电子分布和化学键的形成/断裂有关的性质时理论和实验之间的相互作用。一个很大的重点也致力于化学键的基本方面，以及它的性质如何决定观察到的化学性质和反应性。随着时间分辨（TR）光谱和晶体学研究的出现，特别是在5-10年内，x射线自由电子激光器（XFEL）的国际设施，结构生物学的场景将发生惊人的变化。XFEL将设置第四代x射线源，其脉冲亮度比同步加速器（目前的第三代源）高10个数量级，短3个数量级（几个飞秒）。XFEL将使我们能够获得单分子x射线衍射成像，从而对那些难以结晶甚至不可能结晶的生物大分子或大分子组合进行详细的结构分析。没有晶体的晶体学。接近原子分辨率的三维结构是所有研究结构-功能关系的关键步骤，人类基因组中编码的约30%的蛋白质是几乎不可结晶的膜蛋白。它们也是所有已知药物中约70%的靶标。关于生物复杂系统的结构细节和结构演变的丰富的新的和准确的信息，以及作为其功能基础的反应机制，将逐渐变得可用。本次GRC的九次会议中有四次旨在引起电荷密度（CD）和化学键界的关注，特别是年轻人对这个社区将很快被要求参与的新科学时代的关注。一个在化学键和化学反应性表征、理解和建模的最精细细节方面如此专业的社区，不能与TR研究日益重要和XFEL出现所促进的科学进步分开。相反，它可能会对这种进步作出巨大的、原创性的贡献。本文将讨论目前在大分子和化学反应方面具有开创性的TR光谱和衍射研究，因为它们为在发展中的XFEL源上日益复杂的情况下进行类似的研究奠定了基础。他们还展示了TR衍射如何需要与新的TR光谱技术相结合，以增强我们对生物系统中结构/功能关系的认识。来自这些设施最终建立的地点的演讲者将对XFEL提供的许多基本科学问题进行概述。电荷密度蛋白质数据库将作为一种扩展实验CD方法到生物晶体学的方法进行讨论。如果有关结构和结构演化的信息能提供大分子及其随时间演化的图像，那么对其CD的了解将为理解其为何如此演化提供线索。随着时间分辨光谱学和晶体学的最新进展，特别是5-10年后x射线自由电子激光器国际设备的出现，结构生物学的前景将发生惊人的变化。没有晶体的晶体学将成为可能，这是一个根本性的进步，因为人类基因组中编码的约30%的蛋白质几乎是不可结晶的膜蛋白，而这些蛋白质是所有已知药物中约70%的靶标。这种新的结构信息，以及目前在电荷密度蛋白质数据库中取得的进展，将允许将实验CD方法扩展到生物晶体学；关于结构和结构演化的信息可以提供一个大分子的图像，以及它是如何随时间演化的，而关于它的电荷密度CD的知识将为理解它为何如此演化提供线索。

DESCRIPTION: Gordon Research Conference (GRC) on Electron Distribution and Chemical Bonding. Dynamics and Densities. Mount Holyoke College, South Hadley, MA, USA, 1-6 July 2007. This GRC is traditionally aimed at presenting a forum for discussion on the interplay between theory and experiment when measuring and calculating properties related to electron distribution and the making/breaking of chemical bonds. A large emphasis is also devoted to the fundamental aspects of the chemical bond and how its very nature determines the observed chemical properties and reactivity. With the advent of time-resolved (TR) spectroscopy and crystallographic studies and, especially, in 5-10 years, of the X-ray Free Electron Lasers (XFEL) international facilities, the scenario of structural biology is going to amazingly change. XFEL will set the fourth generation X-ray sources, with pulses about ten orders of magnitude more brilliant and approximately three orders of magnitude shorter, a few femtoseconds, than those provided by synchrotrons - the present third generation sources. XFEL will enable us to obtain single molecule X-ray diffraction imaging and thus a detailed structural analysis of those biologic macromolecules or macromolecular assemblies which are difficult or even impossible to crystallize. A crystallography without crystals. A 3D structure at close to atomic resolution is a key-step for all investigations concerning structure- function relationship and about 30% of the proteins encoded in the humane genome are hardly crystallisable membrane proteins. They are also the target for about 70% of all known drugs. A wealth of new and of accurate information on the structural details and on the structural evolution of biologic complex systems along reactions mechanisms which are at the basis of their functionalities will so become progressively available. Four out of the nine sessions of this GRC are designed to trigger the attention of the charge density (CD) and chemical bond community, especially of younger people, towards the new scientific era this community will be soon asked to take part of. A community, which is so expert in the finest details of chemical bond and chemical reactivity characterization, understanding and modeling can not be set apart from the scientific progress fostered by the increasing importance of TR studies and the advent of XFEL. Instead, it may greatly and originally contribute to such a progress. The present pioneering TR spectroscopic and diffraction studies on macromolecules and chemical reactions will be discussed for they are laying the foundations for similar studies on increasingly complex cases at the developing XFEL sources. They also show how TR diffraction need to be integrated with novel TR spectroscopic techniques to enhance our insight on the structure/function relationships in biological systems. An overview of the many fundamental scientific problems to be afforded with XFEL will be given by speakers coming from the sites where these facilities will be eventually set up. Charge density protein databases will be discusses as a way to extend the experimental CD methodology to biocrystallography. If information on structure and structural evolution yields a picture of a macromolecule and of how it evolves with time, knowledge of its CD will provide a clue to understand why it is so evolving. The scenario of structural biology is going to amazingly change with the recent progresses in time- resolved spectroscopy and crystallography and, especially, with the advent in 5-10 years from now, of the X-ray Free Electron Lasers international facilities. A crystallography without crystals will become feasible, which represents a fundamental progress considering that about 30% of the proteins encoded in the humane genome are hardly crystallisable membrane proteins and that these proteins are the target for about 70% of all known drugs. This new structural information, along with the progresses currently being made in the charge density protein databases will allow to extend the experimental CD methodology to biocrystallography; information on structure and structural evolution yields a picture of a macromolecule and of how it evolves with time, knowledge of its charge density CD will provide a clue to understand why it is so evolving.