机构地区:[1]College of Life Science, Northwest University, Xi'an, Shaanxi 710069, China [2]Weapon Industry 521 Hospital, Xi'an, Shaanxi 710065, China
出 处:《Chinese Journal of Chemistry》2011年第9期1939-1946,共8页中国化学(英文版)
基 金:Project supported by the National Natural Science Foundation of China (No. 21075097).
摘 要:The unfolding of bovine heart cytochrome c induced by urea and guanidine hydrochloride was first studied through intrinsic fluorescence emission spectra and fluorescence phase diagram and the results showed that both of them separately followed a two-state model. As the simplest sample of the unfolding of protein molecules induced by denaturants, an equation was presented to show the effect of the denaturant concentrations in denaturation solu- tion on the residual activity ratios of bovine heart cytochrome c in their two-state unfolding. There are two charac- teristic unfolding parameters K and m in this equation. The former is the thermodynamic equilibrium constant of the unfolding of bovine heart cytochrome c induced by denaturants, the latter is the number of denaturant molecules associated with a bovine heart cytochrome c molecule during the unfolding procedure, and through them the distri- bution and transition of native and completely unfolded bovine heart cytochrome c conformations under different concentrations of urea or guanidine hydrochloride in denaturation solution can be accurately described.The unfolding of bovine heart cytochrome c induced by urea and guanidine hydrochloride was first studied through intrinsic fluorescence emission spectra and fluorescence phase diagram and the results showed that both of them separately followed a two-state model. As the simplest sample of the unfolding of protein molecules induced by denaturants, an equation was presented to show the effect of the denaturant concentrations in denaturation solu- tion on the residual activity ratios of bovine heart cytochrome c in their two-state unfolding. There are two charac- teristic unfolding parameters K and m in this equation. The former is the thermodynamic equilibrium constant of the unfolding of bovine heart cytochrome c induced by denaturants, the latter is the number of denaturant molecules associated with a bovine heart cytochrome c molecule during the unfolding procedure, and through them the distri- bution and transition of native and completely unfolded bovine heart cytochrome c conformations under different concentrations of urea or guanidine hydrochloride in denaturation solution can be accurately described.
关 键 词:bovine heart cytochrome c UNFOLDING distribution and transition fluorescence spectroscopy biologi-cal activity
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