UNDERSTANDING BINDING ENERGY USE

在我们的实验室里，我们已经产生了一种催化抗体 立体选择性地裂解N-甲酰去甲亮氨酸苯酯， 而且效率很高。这种抗体还具有几种 在催化剂中发现的自然进化的特征。这个 特征包括使用活性部位氨基酸来 参与更改绑定顺序，并使用绑定 距离反应中心相对较远的相互作用 有助于促进催化作用。在这个项目中，我们正在研究如何 抗体利用这些远程结合作用来促进催化作用。 这些相互作用非常有趣，因为大多数半抗原设计 已经准备好操作活动站点 反应中心；目前还没有关于这些 远程类型的结合相互作用可以影响催化 催化抗体的作用机制。我们使用的是 计算机图形学实验室将催化剂模型可视化 我们实验室产生的抗体以及其他实验室产生的抗体 (和天然酶)来协助引导定点突变， 和其他蛋白质工程研究。能够使用这些 结构也有助于我们理解结构 抗体催化和蛋白质催化的基础 将军。

In our laboratory, we have generated a catalytic antibody that cleaves the phenyl ester of n-formyl norleucine stereoselectively and with a high efficiency. This antibody also possesses several characteristics found in catalysts that nature has evolved. The characteristics include the use of active site amino acids to participate in bond order changes, and the use o f binding interactions that are relatively remote from the reactive center to help promote catalysis. In this project we are studing how this antibody uses these remote binding interactions to promote catalysis. These interactions are very interesting because most of hapten design has been geared towards manipulating the active site close to the reactive center; there have been no investigations as to how these remote type of binding interaction can influence the catalytic mechanism of catalytic antibodies. We are using the graphics in the Computer Graphics Laboratory to visualize models of the catalytic antibody generated in our lab as well as those generated in other labs (and natural enzymes) to assist in guiding site- directed mutagenesis, and other protein engineering studies. Being able to use these structure is also instrumental in helping us understand the structural basis of antibody catalysis as well as protein based catalysis in general.