REAL-TIME ASSESSMENT OF MACROMOLECULAR INTERACTIONS BY SURFACE PLASMON RESONANCE

大分子与固定化配体结合的探索 测量表面等离子体共振(SPR)的变化 使人们对这些过程是如何发生的有了新的见解。为 例如，全长p51ETS1与其同源基因的实时结合 DNA已被描述为“快开快断”结合，而 相比之下，另一种剪接产物P42 ETS1是一种“慢开慢关”的产品 与相同的同源DNA序列结合。这些蛋白质中的每一个都有 复杂的“状态变化”结合动力学。这样的发现已经 对其他DNA结合蛋白的研究是合理的，以确定 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.