Protein Response to Chromophore Isomerization in Microbial Rhodopsins Revealed by Picosecond Time-Resolved Ultraviolet Resonance Raman Spectroscopy: A Review

Protein Response to Chromophore Isomerization in Microbial Rhodopsins Revealed by Picosecond Time-Resolved Ultraviolet Resonance Raman Spectroscopy: A Review
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皮秒时间分辨紫外共振拉曼光谱揭示微生物视紫红质对发色团异构化的蛋白质反应:综述

DOI:
10.1021/bk-2015-1215.ch016
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发表时间:
2015
期刊:
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy
影响因子:
--
通讯作者:
Y. Mizutani
Y. Mizutani
中科院分区:
--
文献类型:
--
作者:
M. Mizuno;Y. Mizutani

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蛋白质通过改变其结构来发挥功能,外部刺激促进特定结构位点的连续变化。为了理解蛋白质功能的机制,必须阐明外部刺激如何引起这些位点特异性结构变化。时间分辨紫外共振拉曼光谱通过选择性地增强可归属于芳香族氨基酸侧链以及多肽键的振动拉曼带来探测蛋白质结构中特定位点的结构动力学。利用皮秒时间分辨紫外拉曼光谱技术研究了微生物视紫红质中蛋白质对生色团异构化的响应。
Proteins function by changing their structures, and external stimuli facilitate the sequential change of specific structural sites. To understand the mechanism of protein functions, it is essential to clarify how external stimuli can bring about these site-specific structural changes. Time-resolved ultraviolet resonance Raman spectroscopy probes the structural dynamics of specific sites in protein structure by selectively enhancing the vibrational Raman bands assignable to aromatic amino acid side chains as well as polypeptide bonds. We have applied picosecond time-resolved ultraviolet resonance Raman spectroscopy to observation of protein response to chromophore isomerization in microbial rhodopsins.
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