PROTEIN DYNAMICS IN BACTERIORHODOPSIN & RHODOPSIN

这些实验的目的是检测和测量人体的内部运动 细菌视紫红质，随着时间的推移，分辨率为1ps至40ps(初始) 从1ps到1ms，作为蛋白质动力学和蛋白质的探针- 生色团相互作用。建议进行以下实验研究：1) 细菌视紫红质发色团的整体运动幅度和速率 处于光适应状态以及中间体J、K和L；2) 发色团应变构象的松弛；3)活化 生色团运动的障碍；4)温度和溶剂依赖性 结合位几何构型；5)溶剂粘度的依赖关系 生色团弛豫；6)质子配位到邻位酪氨酸 生色团；7)生色团演化的活化体。 低温动力学和常温实验研究 还提出了视紫红质的皮秒构象演化。 我们方法的独特方面是：1)时间制度的可及性 在一台仪器上从1ps到1ms；2)检测内部运动 通过不受激发态限制的各向异性衰变的探测 寿命；3)特定材料松弛速率的详细测量 振动特征；4)温度和压力的精确研究 松弛速率的依赖关系。 提出的方法是使用天然发色团作为蛋白质的探针。 动力学。这个问题被几种皮秒激光技术解决了。 能够生成关于结构和结构的具体和详细信息 动力学。

The aim of these experiments is to detect and measure internal motion in bacteriorhodopsin with 1 ps to 40 ps (initially) resolution over time regimes from 1 ps to 1 ms, as a probe of protein dynamics and protein- chromophore interaction. Experiments are proposed to study: 1) the amplitude and rate of overall motion of the bacteriorhodopsin chromophore in its light-adapted state and in intermediates J, K, and L; 2) the relaxation of strained conformations of the chromophore; 3) activation barriers to chromophore motion; 4) the temperature and solvent dependence of the binding site geometry; 5) the solvent viscosity dependence of chromophore relaxation; 6) proton coordination to a tyrosinate adjacent to the chromophore; and 7) activation volumes for chromophore evolution. Experiments to study low-temperature dynamics and room-temperature picosecond conformational evolution are also proposed for rhodopsin. Unique aspects of our approach are: 1) the accessibility of time regimes from 1 ps to 1 ms on a single instrument; 2) detection of internal motion by a probe of anisotropy decay that is not limited by the excited-state lifetime; 3) detailed measurement of relaxation rates of specific vibrational features; 4) accurate studies of the temperature and pressure dependence of relaxation rates. The approach proposed is to use a natural chromophore as a probe of protein dynamics. This problem is attacked by several picosecond laser techniques capable of generating specific and detailed information about structure and dynamics.