| 半胱氨酸氧化还原状态的协同性 |
| |
| 引用本文： | 宋江宁,李炜疆,须文波.半胱氨酸氧化还原状态的协同性[J].生物物理学报,2004,20(3):233-238. |
| |
| 作者姓名： | 宋江宁 李炜疆 须文波 |
| |
| 作者单位： | 1. 江南大学工业生物技术教育部重点实验室,无锡,214036;江南大学生物工程学院,无锡,214036
2. 江南大学信息工程学院,无锡,214036 |
| |
| 基金项目： | 工业生物技术教育部重点实验室访问学者基金 |
| |
| 摘 要： | 以2002年4月份的Culled Protein Data Bank数据库中的639条蛋白质多肽链为研究对象，统计分析了其含有的584条二硫键的形成特征，发现半胱氨酸氧化还原状态表现出明显的协同性现象：含有二硫键的蛋白质中几乎所有的半胱氨酸都以氧化态形式存在。这一协同性可以通过蛋白质全局水平上的20种氨基酸组分的百分含量很好地加以说明，由此来预测半胱氨酸的氧化还原状态准确率最高可达84．5％。结果表明半胱氨酸是否形成二硫键主要取决于蛋白质全局的而非局部的结构信息。
|
| 关 键 词： | 半胱氨酸 氧化 还原 二硫键 蛋白质折叠 统计分析 |
| 修稿时间： | 2003年9月8日 |
COOPERATIVITY OF THE OXIDIZATION OF CYSTEINES IN GLOBULAR PROTEINS |
| |
| SONG Jiang-ning,Li Wei-jiang,XU Wen-bo.COOPERATIVITY OF THE OXIDIZATION OF CYSTEINES IN GLOBULAR PROTEINS[J].Acta Biophysica Sinica,2004,20(3):233-238. |
| |
| Authors: | SONG Jiang-ning Li Wei-jiang XU Wen-bo |
| |
| Institution: | SONG Jiang-ning1,2,Li Wei-jiang1,2,XU Wen-bo3 |
| |
| Abstract: | 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. |
| |
| Keywords: | Disulfide bond Cysteine Protein folding Statistical analysis Cooperativity |
| 本文献已被 CNKI 维普 万方数据 等数据库收录！ |
| 点击此处可从《生物物理学报》浏览原始摘要信息 |
| 点击此处可从《生物物理学报》下载免费的PDF全文 |
