DEEP UV TRIGGERING OF PROTEIN DYNAMICS

作为我们目标的一部分，产生蛋白质构象的触发物 变化，270 nm的飞秒激光脉冲，蓝宝石第三 谐波，是用来断裂S-S键的，我们研究了小螺旋 对象的结果被约束为非螺旋的束 二硫化桥。由此产生的过程包括螺旋的形成和 巯基自由基的双键复合。两者都是 很有趣，因为它们是由 蛋白质原子。这项工程涉及一项新的紫外线技术。 蛋白质动力学的泵浦和红外探测。这些研究是关于 这些飞秒时间尺度上的系统提供了一个有价值的见解 进入围绕着它们的成对重组的过程中。作为一种 这些实验的延伸，我们已经开发出技术来 探索这些多肽在8个数量级以上的动力学 超时到毫秒时间刻度。温度和阿尔法的影响 螺旋促进剂(如三氟乙醇)现在正在 对这些体系的动力学进行了研究。

As part of our goal to generate triggers of protein conformational changes, femtosecond laser pulses at 270nm, the Tisapphire 3rd harmonic, are utilized to break S-S bonds we studied small helix bundles that are constrained to be non-helical as a result of the disulfide bridge. The resulting processes involve helix formation and geminate recombination of the sulfhydryl radicals. Both are interesting since they are controlled by the fluctuations of the protein atoms. This project involves a new technology of ultraviolet pumping and infrared probing of protein dynamics. These studies of these systems on a femtosecond timescale have lent a valuable insight into the processes surrounding their geminate recombination. As an extension of these experiments, we have developed technologies to probe the dynamics of these peptides over 8 orders of magnitude in time out to the ms time scale. The effect of temperature and alpha helix promoting solvents (such as trifluoro ethanol) are now being investigated on the kinetics of these systems.