Micro-environmental influences on the fluorescence of tryptophan.
The fluorescence characteristics of protein molecules are mainly due to their tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) residues, among which tryptophan is the most important. Studying the influence of the micro-environment on tryptophan fluorescence can give us direct and convincing evidence for changes of protein structure and function. In this paper, fluorescence spectroscopy was used to evaluate the changes of tryptophan fluorescence under a variety of micro-environmental conditions (temperature, pH, polarity, presence of surfactants and oxidants) and the mechanisms responsible. This study not only presents more direct evidence to explain how and why the protein fluorescence spectra change, but also provides a new method for analyzing the effect of environmental changes on protein function.
Sun
Feng
F
School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100, Shandong, PR China.
Zong
Wansong
W
Liu
Rutao
R
Chai
Jun
J
Liu
Ying
Y
D006863:Hydrogen-Ion Concentration; D016877:Oxidants / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013501:Surface-Active Agents / Q000737:chemistry; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry*
D016877:Oxidants; D013501:Surface-Active Agents; D014364:Tryptophan