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Nanosecond-time-resolved infrared spectroscopic study of fast relaxation kinetics of protein folding by means of laser-induced temperature-jump
作者姓名:张庆利  王莉  翁羽翔  邱祥冈  王渭池  阎吉祥
作者单位:Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;Beijing Institute of Technology, Beijing 100080,China;Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;National Laboratory for Superconductivity, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;Beijing Institute of Technology, Beijing 100080,China
基金项目:Project supported by the National Natural Science Foundation of China (Grant No 20373088) and Program for innovation group (Grant No 60321002).
摘    要:Elucidating the initial kinetics of folding pathways is critical to the understanding of the protein folding mechanism. Transient infrared spectroscopy has proved a powerful tool to probe the folding kinetics. Herein we report the construction of a nanosecond laser-induced temperature-jump (T-jump) technique coupled to a nanosecond timeresolved transient mid-infrared (mid-IR) spectrometer system capable of investigating the protein folding kinetics with a temporal resolution of 50 ns after deconvolution of the instrumental response function. The mid-IR source is a liquid N2 cooled CO laser covering a spectral range of 5.0μm (2000 cm^-1)-6.5μm (1540 cm^-1). The heating pulse was generated by a high pressure H2 Raman shifter at wavelength of 1.9μm. The maximum temperature-jump could reach as high as 26±1℃. The fast folding/unfolding dynamics of cytochrome C was investigated by the constructed system, providing an example.

关 键 词:微秒  纳秒  激光诱导升温  瞬时红外光谱  动力学
收稿时间:7/6/2005 12:00:00 AM
修稿时间:9/8/2005 12:00:00 AM

Nanosecond-time-resolved infrared spectroscopic study of fast relaxation kinetics of protein folding by means of laser-induced temperature-jump
Zhang Qing-Li,Wang Li,Weng Yu-Xiang,Qiu Xiang-Gang,Wang Wei-Chi and Yan Ji-Xiang.Nanosecond-time-resolved infrared spectroscopic study of fast relaxation kinetics of protein folding by means of laser-induced temperature-jump[J].Chinese Physics B,2005,14(12):2484-2490.
Authors:Zhang Qing-Li  Wang Li  Weng Yu-Xiang  Qiu Xiang-Gang  Wang Wei-Chi and Yan Ji-Xiang
Institution:Beijing Institute of Technology, Beijing 100080,China; Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China;Beijing Institute of Technology, Beijing 100080,China; Laboratory of Soft Matter Physics, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China; National Laboratory for Superconductivity, Institute of Physics,Chinese Academy of Sciences, Beijing 100080, China
Abstract:Elucidating the initial kinetics of folding pathways is critical to the understanding of the protein folding mechanism. Transient infrared spectroscopy has proved a powerful tool to probe the folding kinetics. Herein we report the construction of a nanosecond laser-induced temperature-jump ($T$-jump) technique coupled to a nanosecond time-resolved transient mid-infrared (mid-IR) spectrometer system capable of investigating the protein folding kinetics with a temporal resolution of 50 ns after deconvolution of the instrumental response function. The mid-IR source is a liquid N$_{2}$ cooled CO laser covering a spectral range of 5.0$\mu$m (2000 cm$^{-1}) \sim $ 6.5$\mu$m (1540 cm$^{-1})$. The heating pulse was generated by a high pressure H$_{2}$ Raman shifter at wavelength of 1.9$\mu$m. The maximum temperature-jump could reach as high as 26$\pm $1$^{\circ}$C. The fast folding/unfolding dynamics of cytochrome $C$ was investigated by the constructed system, providing an example.
Keywords:protein folding  sub-microsecond  laser-induced temperature-jump  transient infrared\linebreak \hbox{\hskip 1  9cm} spectrum  dynamics  cytochrome $C$
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