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ISSN 1000-6818CN 11-1892/O6CODEN WHXUEU
Acta Phys Chim Sin >> 0,Vol.>> Issue()>> 0-0     doi: 10.3866/PKU.WHXB201703061         中文摘要
Accepted manuscript
Fluorescence Dynamics of LicT Protein by Time-resolved Spectroscopy
CHANG Meng-Fang1, LI Lei1, CAO Xiao-Dan1, JIA Meng-Hui2, ZHOU Jia-Sheng1, CHEN Jin-Quan1, XU Jian-Hua1
1 State Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, P. R. China;
2 Chinese Academy of Sciences, Shanghai Institute of Optics and Fine Mechanics, Shanghai 201800, P. R. China
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In this paper, the fluorescence dynamics of tryptophan residues in the LicT protein were determined by time-resolved fluorescence spectroscopy combined with UV absorption and steady-state fluorescence spectroscopy. Moreover, the local microenvironment and structural changes of LicT protein before and after activation were studied. The activated LicT protein, AC 141, prevents the transcriptional antitermination of genes involved in carbohydrate utilization, which accelerates the organism's metabolism. The structural properties and microenvironment of AC 141 and the wild-type protein, Q 22, were determined by differences in the wavelength/intensity of tryptophan-associated fluorescence emissions, as well as in the lifetimes of these emissions. The interaction between tryptophan residues and the solvent was elucidated by decay-associated spectroscopy (DAS) and time-resolved emission spectra (TRES). These methods indicate that, upon activation, the structure of AC 141 is more compact than that of wild-type Q 22. In addition, TRES also showed that tryptophan residues in the protein had a continuous spectral relaxation process. Anisotropy experiments, which illustrate the conformational motions of amino acid residues and whole proteins, suggested that tryptophan residues had independent local motions in the protein system, and that the motions were more intense in the activated protein.



Keywords: Time-correlated single-photon counting   Tryptophan   Decay-associated spectra   Time-resolved emission spectra   Anisotropy  
Received: 2017-01-05 Accepted: 2017-03-01 Publication Date (Web): 2017-03-06
Corresponding Authors: XU Jian-Hua Email: jhxu@ecnu.edu.cn


Cite this article: CHANG Meng-Fang, LI Lei, CAO Xiao-Dan, JIA Meng-Hui, ZHOU Jia-Sheng, CHEN Jin-Quan, XU Jian-Hua. Fluorescence Dynamics of LicT Protein by Time-resolved Spectroscopy[J]. Acta Phys. -Chim. Sin., 0, (): 0-0.    doi: 10.3866/PKU.WHXB201703061

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