大豆Em(LEA1)蛋白保守结构域的结构和聚集特性  

Structures and Assembly of Conserved Domains from Soybean Late Embryogenesis Abundant Protein Em

作　　者：薛蓉[1] 邹永东[2] 郑易之[2] 吴亦洁[1] 李晓晶[1] 裴奉奎[1] 

机构地区：[1]中国科学院长春应用化学研究所,长春130022 [2]深圳大学生命科学学院,深圳市微生物基因工程重点实验室,深圳518060

出　　处：《分析化学》2012年第4期563-568,共6页Chinese Journal of Analytical Chemistry

基　　金：中车博士后基金(No.20100471273);国家自然科学基金(Nos.31070230,20095097)资助项目

摘　　要：采用圆二色谱(CD)和核磁共振波谱(NMR)方法研究了大豆Em(LEA1)蛋白保守基序Em-C和Em-2M多肽在不同环境中的结构及聚集行为。研究表明,在水和DMPG溶液中,两种多肽主要以无规结构形式存在。在50%TFE溶液中,Em-C多肽折叠结构增加,含疏水残基的部分区域可能形成α-螺旋结构,且分子以二聚体形式存在;而Em-2M则以单体形式存在,且有序结构较少。以上结果表明,环境变化可能导致两种多肽的空间结构和聚集行为改变,这有助于理解Em蛋白在不同环境中的结构特点,及其重要区域在全长蛋白中所起的作用。In this study,we investigated the structures and assembly of C domain of soybean late embryogenesis abundant（LEAI） protein EM（Em-C） and M domain of soybean LEAI protein EM（Em-2M） from the soybean LEA1 protein Em in different environments using CD and NMR spectroscopy.In water and dimyristoylphosphatidyglycerol（DMPG） solution,both peptides were predominantly disordered.In 50% 2,2,2-trifluoroethanol（TFE） aqueous solution,Em-C had increasing folding and self-assembled as dimer,and the region including hydrophobic residues might form helical structure.Em-2M formed less ordered structure than Em-C and existed as monomer in 50% TFE aqueous solution.These results suggested that the change of environment might lead to variation of spatial structure and assembly behavior for the two peptides Em-C and Em-2M.The present study may provide an insight into the structural properties of Em protein in different environments and the roles of some important segments in Em protein.

关 键 词：晚期胚胎发生富集(LEA1)蛋白 核磁共振 结构 聚集 

分 类 号：S565.1[农业科学—作物学]