DEEP UV TRIGGERING OF PROTEIN DYNAMICS

深紫外触发蛋白质动力学

• 批准号: 6328019
• 负责人: M VOLK
• 金额: $ 1.09万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-08-01 至 2001-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6328019
• 关键词: biological products; biomedical equipment development; biomedical resource; technology /technique

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.

作为我们目标的一部分， 变化，飞秒激光脉冲在270 nm，Tisapphire第三代 谐波，用来打破S-S键，我们研究了小螺旋 束被约束为非螺旋的结果， 二硫桥 由此产生的过程涉及螺旋形成和 巯基的成对重组。 两者都是 有趣的是，因为它们是由波动控制的。 蛋白质原子 这个项目涉及一种新的紫外线技术 泵送和红外探测蛋白质动力学。 这些研究 这些飞秒时间尺度上的系统提供了宝贵的见解 它们的双生重组过程。 作为 这些实验的延伸，我们已经开发出技术， 探测这些肽的动力学超过8个数量级， 超时到ms时标。 温度和α的影响 螺旋促进溶剂（如三氟乙醇）现在正被 研究了这些系统的动力学。