%0 Journal Article
%T COOPERATIVITY OF THE OXIDIZATION OF CYSTEINES IN GLOBULAR PROTEINS<br>半胱氨酸氧化还原状态的协同性
%A SONG Jiang-ning
%A Li Wei-jiang
%A XU Wen-bo
%A <br>宋江宁
%A 李炜疆
%A 须文波
%J 生物物理学报
%D 2004
%I 
%X Based on the PISCES culled Protein Data Bank with 639 protein polypeptide chains and 584 disulfide bonds in April 2002, the formation feature of disulfide connectivity was statistically analyzed. The oxidation of cysteines exhibited obvious cooperativity: almost all cysteines in disulfide-bond containing proteins were in the oxidized form. This cooperativity could be well described by the amino acid composition, based on which the prediction of the oxidation form of cysteines reached an accuracy above 84.5%. It was showed that whether cysteines should form disulfide bonds depended mainly on the global but not local structural features of proteins. The result demonstrated the applicability of this new simple method for the prediction of the oxidation states of cysteines in proteins.
%K Disulfide bond
%K Cysteine
%K Protein folding
%K Statistical analysis
%K Cooperativity<br>半胱氨酸
%K 氧化
%K 还原
%K 二硫键
%K 蛋白质折叠
%K 统计分析
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=2EE2745D36FBCA7D&yid=D0E58B75BFD8E51C&vid=A04140E723CB732E&iid=38B194292C032A66&sid=FD7C952458BFB5D8&eid=9CA95D22FC1D537C&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=15