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Conformational changes and surface binding property of rat liver Cd_5Zn_2-metallothionein
作者姓名:HUANG  Zhong-Xian GU  Wei-Qiang ZHENG  Qi LIU  Fang SUN  Yao-Jun
作者单位:HUANG,Zhong-Xian GU,Wei-Qiang ZHENG,Qi LIU,Fang SUN,Yao-JunDepartment of Chemistry,Fudan University,Shanghai ?0433,China
基金项目:Project supported by the National Natural Science Foundation of China and the Doctoral Program Foundation of National Education Commission of China
摘    要:A series of conformational changes of native rat liver metallothionein were observedunder different ionic strength by 1H NMR. Furthermore, binding of magnetic probes to MT gives us an implication that positively charged groups of lysine are not completely folded back towards the inner core of metallothionein, the negatively charged metal-sulfur core is slightly exposed to the solvent.


Conformational changes and surface binding property of rat liver Cd_5Zn_2-metallothionein
HUANG,Zhong-Xian GU,Wei-Qiang ZHENG,Qi LIU,Fang SUN,Yao-Jun.Conformational changes and surface binding property of rat liver Cd_5Zn_2-metallothionein[J].Chinese Journal of Chemistry,1997,15(5):385-394.
Authors:HUANG  Zhong-Xian GU  Wei-Qiang ZHENG  Qi LIU  Fang SUN  Yao-Jun
Institution:HUANG,Zhong-Xian GU,Wei-Qiang ZHENG,Qi LIU,Fang SUN,Yao-JunDepartment of Chemistry,Fudan University,Shanghai ?0433,China
Abstract:A series of conformational changes of native rat liver metallothionein were observedunder different ionic strength by 1H NMR. Furthermore, binding of magnetic probes to MT gives us an implication that positively charged groups of lysine are not completely folded back towards the inner core of metallothionein, the negatively charged metal-sulfur core is slightly exposed to the solvent.
Keywords:Rat liver metallothionein  NMR studies of protein  magnetic relaxation probe
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