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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Skeletal Structure of the Chromophore of Photoactive Yellow Protein in the Excited State Investigated by Ultraviolet Femtosecond Stimulated Raman Spectroscopy
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Skeletal Structure of the Chromophore of Photoactive Yellow Protein in the Excited State Investigated by Ultraviolet Femtosecond Stimulated Raman Spectroscopy

机译：通过紫外线刺激拉曼光谱研究激发态激活黄蛋白发色团的骨骼结构

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摘要

We studied ultrafast structural dynamics of photoactive yellow protein (PYP) using ultraviolet femtosecond stimulated Raman spectroscopy. By employing the Raman pump and probe pulses in the ultraviolet region, resonantly enhanced, rich vibrational features of the excited-state chromophore were observed in the fingerprint region. In contrast to the marked spectral change reported for the excited-state chromophore in solution, in the protein, all of the observed Raman bands in the fingerprint region did not show any noticeable spectral shifts nor band shape changes during the excited-state lifetime of PYP. This indicates that the significant skeletal change does not occur on the chromophore in the excited state of PYP and that the trans conformation is retained in its lifetime. Based on the femtosecond Raman data of PYP obtained so far, we discuss a comprehensive picture of the excited-state structural dynamics of PYP.
机译：利用紫外飞秒受激拉曼光谱研究了光活性黄蛋白（PYP）的超快结构动力学。通过在紫外区域使用拉曼泵和探测脉冲，在指纹区域观察到激发态发色团的共振增强和丰富的振动特征。与溶液中激发态发色团的显著光谱变化相反，在蛋白质中，在PYP的激发态寿命期间，指纹区域中观察到的所有拉曼谱带均未显示任何明显的光谱位移或谱带形状变化。这表明，在PYP的激发态下，发色团没有发生显著的骨架变化，并且反式构象在其寿命期内保持不变。基于迄今为止获得的PYP的飞秒拉曼数据，我们讨论了PYP激发态结构动力学的综合图像。

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