RUI: Fundamental Processes of Protein Crystallization and acromolecular Assembly

这项研究的长期目标是了解生物大分子有序组装形成的机制。这些对称的结构是由彼此具有特定的、重复的相互作用的分子组成的。它们既包括延伸的结构，如细胞骨架细丝和膜光感受器阵列，也包括紧凑的结构，如核孔复合体和病毒。它们在细胞形态、运动和其他细胞功能领域发挥着至关重要的作用。要研究的问题是：这种有序结构是如何自我组装的，即组成分子如何找到途径，识别并附着到特定的位置？更直接的目标是将新兴的原子力显微镜技术应用于模型自组装系统，即三维蛋白质晶体。除了构成有序组装的简单情况外，结晶通常是X射线衍射法测定蛋白质结构的限速步骤。为了制定合理的指导方针来优化晶体生长，德宾博士建议研究结晶的基本过程。蛋白质晶体在发展和应用原子力显微镜方法成像生物分子和结构方面具有独特的优势。

The long term goal of this research is to understand the mechanisms by which ordered assemblies of biological macromolecules are formed. These symmetrical structures are made up of molecules having specific, repeated interactions with each other. They include both extended structures, such as cytoskeletal filaments and membrane photoreceptor arrays, and compact ones, such as nuclear pore complexes and viruses. They play crucial roles in cell morphology, motility, and other areas of cell function. The question to be investigated is: how do such ordered structures assemble themselves, i.e. how do the component molecules find their way to, recognize, and attach to specific sites? The more immediate aim is to apply the emerging technique of atomic force microscopy to a model self-assembling system, a three-dimensional protein crystal. Besides constituting a simple case of ordered assembly crystallization is generally the rate-limiting step in determining protein structure by X-ray diffraction. To develop rational guidelines for optimizing crystal growth, Dr. Durbin proposes to study the fundamental process of crystallization. Protein crystals have unique advantages for developing and applying methods of atomic force microscopy to imaging biological molecules and structures.