%0 Journal Article
%T FT-IR STUDIES OF α-ASPARTYL DIPEPTIDASE AND ITS EVOLUTIONAL ENZYME<br>α-天门冬氨酰二肽酶及其进化酶的FT-IR 研究
%A LI Zheng-qiang
%A HUANG Pin-wei
%A TAO Yan-chun
%A LIU Wei
%A LU Ming
%A ZHANG Jin
%A <br>李正强
%A 黄品伟
%A 陶艳春
%A 刘嵬
%A 吕明
%A 张今
%J 生物物理学报
%D 2002
%I 
%X Under double screen pressure of specific activity and thermo stablity, an evolved α-aspartyl dipeptidase, with 47 folds higher activity than its wild type ancestor, was obtained. By using FT-IR, the secondary structure of α-aspartyl dipeptidase and its evolutional enzyme were studied. It is found that α-helix structure is 31%,β-sheet content is 26.8% while turn and random coil component are 42.2% in the evolutional type of α-aspartyl dipeptidase .In the wild type enzyme, α-helix structure is 33%, β-sheet content is 28.5% and turn and random coil are 38.5%.These structure changes lead to arise the flexibility of evolutional type and adaptability to substrate.
%K aspartyl dipeptidase
%K Evolutional enzyme
%K FT-IR
%K Secondary structure<br>α－天门冬氨酰二须酶
%K 进化酶
%K FT－IR研究
%K 二级结构
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=1E2A5C3F27AA11F9&yid=C3ACC247184A22C1&vid=13553B2D12F347E8&iid=0B39A22176CE99FB&sid=23104246A5FCFCEF&eid=E0F6F365E4766526&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=6