Engineering Protein Separations on Immobilized Metals

利用生物亲和性来实现分离是许多有前途的工艺的基础。亲和力概念的一个特别吸引人的版本利用蛋白质和固定金属之间的相互作用。主要研究人员提出了一种新的方法来解决蛋白质纯化问题，基于他们使用遗传方法设计特定蛋白质结构的能力。他们打算用两种表面性质和构象截然不同的蛋白质来证明，特定的金属结合位点确实可以被整合到蛋白质中，或者作为可移动的“尾巴”附着在蛋白质上，而不会失去生物活性或折叠结构。有了这种改变，蛋白质就有可能在含金属的聚合物基质上进行一步纯化。

The utilization of biological affinity to effect a separation is the basis of a number of promising processes. A particularly attractive version of the affinity concept utilizes interactions between proteins and immobilized metals. The principal investigators propose a novel approach to the problem of protein purification based on their ability to engineer specific protein structures using genetic methods. They propose to demonstrate, using two proteins of very different surface properties and conformations, that specific metal binding sites can indeed be incorporated into proteins or attached as removable "tails" without loss of biological activity or folded structure. With this alteration, proteins can possibly be engineered for a single- step purification on metal-containing polymer matrices.