高等学校化学学报

高等学校化学学报 ›› 1999, Vol. 20 ›› Issue (S1): 345.

• Molecular Spectroscopy • 上一篇    下一篇

Study on Conformation of Escherichia Coli Alkaline Phosphatase by Intrinsic tryptophan Room Temperature Phosphorescence Probe

ZHANG Hai-Rong, NIU Cheng-Gang, DONG Chuan, JIN Wei-Jun, LIU Chang-Song   

  1. Department of Chemistry, Shanxi Univwesiiy, Taiyuan, 030006, P. R. China
  • 出版日期:1999-12-31 发布日期:1999-12-31
  • 基金资助:

    This work was supported by the NNSF and Shanxi Province Youth Fooundation.

Study on Conformation of Escherichia Coli Alkaline Phosphatase by Intrinsic tryptophan Room Temperature Phosphorescence Probe

ZHANG Hai-Rong, NIU Cheng-Gang, DONG Chuan, JIN Wei-Jun, LIU Chang-Song   

  1. Department of Chemistry, Shanxi Univwesiiy, Taiyuan, 030006, P. R. China
  • Online:1999-12-31 Published:1999-12-31
  • Supported by:

    This work was supported by the NNSF and Shanxi Province Youth Fooundation.

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摘要：

Room temperature phosphorescence(RTP) probe is a powerful tool for studying the kinetics and relationship between the conformation change and physiological function of protein because some slow kinetic processes of protein in solution just occur the same time scales as phosphorescence lifetime and it susceptibly indicates microenvironment properties. RTP of Escherichia coli alkaline phosphatase(AP) comes mainly from tryptophan residues (Trp-109). It is well known that the deeper Trp-109 is embedded, The stronger phosphorescence emitting is, and the longer its lifetime is. The current work is a preliminary study of the conformation changes of AP, the local microenvironment of Trp-109 and the quenching kinetic natures in the unfolded processes of AP in the presence of different denaturants.

Abstract:

Room temperature phosphorescence(RTP) probe is a powerful tool for studying the kinetics and relationship between the conformation change and physiological function of protein because some slow kinetic processes of protein in solution just occur the same time scales as phosphorescence lifetime and it susceptibly indicates microenvironment properties. RTP of Escherichia coli alkaline phosphatase(AP) comes mainly from tryptophan residues (Trp-109). It is well known that the deeper Trp-109 is embedded, The stronger phosphorescence emitting is, and the longer its lifetime is. The current work is a preliminary study of the conformation changes of AP, the local microenvironment of Trp-109 and the quenching kinetic natures in the unfolded processes of AP in the presence of different denaturants.

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