Toll作用蛋白C2结构域的纯化和结构研究  

Purificaiton and structure study of C2 domain in Toll interacting protein

作　　者：肖淑艳 董忠平 

机构地区：[1]内蒙古科技大学材料与冶金学院,内蒙古包头014010

出　　处：《内蒙古科技大学学报》2017年第4期307-311,共5页Journal of Inner Mongolia University of Science and Technology

基　　金：内蒙古自治区自然科学基金资助项目(2015BS0205);国家自然科学基金资助项目(21663017)

摘　　要：在大肠杆菌中高表达了谷胱甘肽S转移酶(GST)-Toll作用蛋白C2结构域融合蛋白,并通过GST磁珠纯化融合蛋白,用凝血酶把GST和C2结构域切开,采用尺寸排阻色谱纯化了C2结构域.用圆二色谱和核磁共振波谱法研究了C2结构域在三羟甲基氨基甲烷盐酸缓冲液中的结构,结果表明C2结构域在缓冲液中形成了以β折叠为主的结构.Toll interacting protein C2 domain was overexpressed in Escherichia coli as an Glutathione S-Transferase( GST) fusion protein. The fusion protein was purified using glutathione beads,and C2 domain was released from GST using thrombin and then purified by size exclusion chromatography. The structure of Toll interacting protein C2 domain in Tris-HCl buffer were investigated by CD and NMR spectroscopy. The study shows that C2 domain presents a predominately β-sheet structure in buffer.

关 键 词：Toll作用蛋白 C2结构域 纯化 结构 

分 类 号：O629.7[理学—有机化学]