2007 Electron Distribution & Chemical Bonding Gordon Research Conference

戈登研究会议（GRC）电子分布和化学键。动力学和密度。2007年7月1日至6日，美国马萨诸塞州南哈德利霍利奥克山学院。这个GRC传统上旨在提供一个论坛，讨论理论和实验之间的相互作用，测量和计算与电子分布和化学键的形成/断裂相关的性质。一个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）光谱学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（XFEL）国际设施的出现，结构生物学的情况将发生惊人的变化。XFEL将设置第四代X射线源，其脉冲比同步加速器（目前的第三代源）提供的脉冲亮度高出约10个数量级，短约3个数量级，即几飞秒。XFEL将使我们能够获得单分子X射线衍射成像，从而对那些难以甚至不可能结晶的生物大分子或大分子组装体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3D结构是所有关于结构-功能关系的研究的关键步骤，并且人类基因组中编码的约30%的蛋白质是难以结晶的膜蛋白。它们也是大约70%的已知药物的靶点。关于生物复杂系统的结构细节和结构演变的大量新的和准确的信息，将沿着作为其功能基础的反应机制沿着逐渐变得可用。本次GRC的九个会议中有四个旨在引发电荷密度（CD）和化学键社区，特别是年轻人对新科学时代的关注，这个社区将很快被要求参加。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，它可能会大大地和最初地有助于这种进步。目前开创性的TR光谱和衍射研究的大分子和化学反应将被讨论，因为他们正在为类似的研究在日益复杂的情况下，在发展中的XFEL源奠定了基础。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/功能关系的洞察力。XFEL将提供的许多基本科学问题的概述将由来自这些设施最终将建立的地点的发言者给出。电荷密度蛋白质数据库将被讨论作为一种方式来扩展实验CD方法，以biocompellulallography。如果关于结构和结构进化的信息产生了一幅关于大分子及其如何随时间进化的图像，那么关于其CD的知识将提供一条线索来理解它为什么如此进化。随着时间分辨光谱学和晶体学的最新进展，特别是随着5-10年后X射线自由电子激光国际设施的出现，结构生物学的情况将发生惊人的变化。没有晶体的晶体学将变得可行，这代表了一个根本性的进步，考虑到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，并且这些蛋白质是约70%的已知药物的靶点。这一新的结构信息，沿着目前正在取得的进展，在电荷密度蛋白质数据库将允许扩展的实验CD方法的biocompatibilallography;结构和结构演变的信息产生一个大分子的图片，它是如何随着时间的推移而演变，其电荷密度CD的知识将提供一个线索，以了解为什么它是如此演变。

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.