2007 Electron Distribution & Chemical Bonding Gordon Research Conference

描述：戈登研究会议(GRC)关于电子分布和化学键。动态和密度。曼荷莲学院，南哈德利，美国马萨诸塞州，2007年7月1日至6日。传统上，GRC的目的是提供一个论坛，讨论在测量和计算与电子分布和化学键的建立/断开有关的性质时，理论和实验之间的相互作用。重点还放在化学键的基本方面，以及它的性质如何决定观察到的化学性质和反应性。随着时间分辨光谱学和结晶学研究的出现，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，结构生物学的情景将发生惊人的变化。XFEL将设置第四代X射线源，其脉冲比目前的第三代源--同步加速器提供的脉冲亮度高约十个数量级，短约三个数量级，甚至几飞秒。XFEL将使我们能够获得单分子X射线衍射成像，从而对那些难以结晶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。没有晶体的结晶学。接近原子分辨率的三维结构是研究结构-功能关系的关键步骤，人类基因组中编码的大约30%的蛋白质几乎不是结晶膜蛋白。它们也是约70%已知药物的靶标。因此，关于生物复杂系统的结构细节和结构演化的大量新的和准确的信息将逐渐变得可用，这些信息是基于其功能的反应机制。在这次GRC的九次会议中，有四次旨在引发电荷密度(CD)和化学键社区，特别是年轻人的注意，走向这个社区即将被要求参与的新科学时代。一个在化学键和化学反应活性表征、理解和建模的最详细细节方面如此专业的社区，与TR研究日益重要和XFEL的出现所促进的科学进步是分不开的。相反，它可能会对这样的进步做出巨大的、最初的贡献。将讨论目前开创性的大分子和化学反应的TR光谱和衍射研究，因为它们为正在开发的XFEL源上日益复杂的情况的类似研究奠定了基础。它们还展示了如何将TR衍射与新的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。来自最终建立这些设施的地点的演讲者将概述XFEL将提供的许多基本科学问题。电荷密度蛋白质数据库将作为将实验CD方法扩展到生物晶体学的一种方式进行讨论。如果关于结构和结构演化的信息产生了一幅大分子的图景以及它是如何随时间演化的，那么对其CD的了解将为理解它为什么如此演化提供线索。随着时间分辨光谱学和结晶学的最新进展，结构生物学的情景将发生惊人的变化，特别是随着5-10年后X射线自由电子激光国际设施的到来。没有晶体的结晶学将成为可能，这是一个根本性的进步，考虑到人类基因组中编码的大约30%的蛋白质几乎不是可结晶的膜蛋白，而且这些蛋白质是所有已知药物的靶标约70%。这种新的结构信息，加上目前在电荷密度蛋白质数据库中取得的进展，将使CD实验方法能够扩展到生物结晶学；关于结构和结构演变的信息产生了一幅大分子的图景以及它是如何随时间演变的，关于其电荷密度CD的知识将为理解它为什么如此演变提供线索。

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.