STATIC VS COLLISIONAL QUENCHING OF TRYPTOPHAN EMISSION DUE TO HALOTHANE

我们正在了解全身麻醉剂如何与 proteins. 荧光猝灭法已被开发， 研究这个问题。 挥发性全身麻醉剂氟烷是 用缓冲液平衡并以预定稀释度添加至 蛋白质溶液和天然色氨酸荧光猝灭， 测定了 在甲醇溶液中，色氨酸的荧光被猝灭 通过氟烷在高得多的溶剂相浓度下 麻醉剂 荧光猝灭本质上是碰撞的， 可能是由麻醉剂上的溴原子引起的 的 蛋白质数据的解释是氟烷分配到 在吲哚环附近的疏水结构域。 问题 我们要回答的是，这是否是一个静态（意味着特定的 结合到蛋白质）或碰撞淬灭过程 氟烷-蛋白质相互作用 时间分辨荧光寿命 测量允许静态和碰撞淬火， 杰出的

We are understanding how general anesthetics interact with proteins. A fluorescence quenching method has been developed to examine this question. The volatile general anesthetic halothane is equilibrated with buffer and added at predetermined dilutions to a protein solution and the native tryptophan fluorescence quenching is measured. ree L-tryptophan fluorescence in methanol can be quenched by halothane at much higher concentrations of solvent phase anesthetic. The fluorescence quenching is collisional in nature and is probably caused by the bromine atom on the anesthetic. The interpretation of the protein data is that halothane partitions into hydrophobic domains in the vicinity of the indole rings. The question we are answering is whether this is a static (implying specific binding to the protein) or collisional quenching process for the halothane-protein interaction. Time resolved fluorescence lifetime measurements are allowing static and collisional quenching to be distinguished.