REAL-TIME ASSESSMENT OF MACROMOLECULAR INTERACTIONS BY SURFACE PLASMON RESONANCE

利用固定化配体与大分子结合的研究 测量表面等离子体共振（SPR）的变化 对这些过程如何发生有了新的认识。 为 例如，全长p51 ETS1与其同源物的实时结合 DNA的特征是“快速开启，快速关闭”结合，而 相反，交替剪接产物p42 ETS1是一种“慢开慢关”的蛋白， 与相同的同源DNA序列结合。 这些蛋白质中的每一种都有 复杂的“状态变化”结合动力学。 这些发现有 证明了其他DNA结合蛋白的研究，以确定是否 SPR测量可以区分不同的动力学机制。

The exploration of macromolecular binding to immobilized ligands through the measurement of changes in surface plasmon resonance (SPR) measured in real-time has given new insight into how these processes occur. For example, the real-time binding of the full-length p51 ETS1 to its cognate DNA has been characterized as 'fast-on, fast off' binding while by contrast, the alternate splice product, p42 ETS1 is a 'slow-on, slow off' binder to the same cognate DNA sequence. Each of these proteins has complex, "change-of-state" binding kinetics. Such findings have justified studies of other DNA binding proteins in order to determine if SPR measurements could distinguish different kinetic mechanisms.