Luminescence diagnostics of conformational changes of the Hsp70 protein in the course of thermal denaturation

被引：5
|
作者：
Bukina, M. N. [1 ]
Bakulev, V. M. [1 ]
Barmasov, A. V. [1 ]
Zhakhov, A. V. [2 ]
Ishchenko, A. M. [2 ]
机构：
[1] St Petersburg State Univ, St Petersburg 199034, Russia
[2] State Res Inst High Pur Biopreparat, St Petersburg 197110, Russia
来源：
OPTICS AND SPECTROSCOPY | 2015年 / 118卷 / 06期
关键词：
Tryptophan; Quantum Yield; Luminescence Spectrum; Luminescence Intensity; Aromatic Amino Acid;
D O I：
10.1134/S0030400X15060065
中图分类号：
O43 [光学];
学科分类号：
070207 ; 0803 ;
摘要：
The spectral luminescence properties of aqueous solutions of the Hsp70 protein are studied, the dependence of the luminescence spectrum on the excitation wavelength is revealed, and the temperature dependence of luminescence intensity of tyrosine and tryptophan residues in the temperature interval of 20-80A degrees C is analyzed. The luminescence method is used to determine temperature interval (42-57A degrees C) in which protein melting takes place. An increase in the fluorescence quantum yield of tryptophan and the bathochromic shift of the emission spectrum of denatured Hsp70 prove that transition takes place of tryptophanyls to the surface of the protein molecule.
引用
收藏
页码：899 / 901
页数：3
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