| 一种表征蛋白质可分泌性的结构融合度特征 |
| |
| 引用本文： | 高翠芳,吴小俊,田丰伟,夏雨,陈卫.一种表征蛋白质可分泌性的结构融合度特征[J].生物工程学报,2010,26(5):687-695. |
| |
| 作者姓名： | 高翠芳 吴小俊 田丰伟 夏雨 陈卫 |
| |
| 作者单位： | 1. 江南大学信息工程学院,无锡,214122
2. 江南大学食品学院,食品科学与技术国家重点实验室,无锡,214122 |
| |
| 基金项目： | 教育部新世纪优秀人才计划项目 (No. NCET-06-0487)，国家自然科学基金 (Nos. 60572034, 60973094, 30670065)，江苏省自然科学基金 (No. BK2006081)，江南大学创新团队计划项目 (No. JNIRT0702) 资助。 |
| |
| 摘 要： | 选择适宜的信号肽是实现外源蛋白高效分泌表达的一个重要因素。本研究利用生物信息学方法分析信号肽与外源蛋白之间的相容程度，将其定义为结构融合度，并从数学角度分析拼接信号肽与目的蛋白邻近残基之间的相互作用，提出了信号肽拼接区域与目标蛋白之间的数学模型，利用该模型进行结构融合度特征提取，以此来表征外源蛋白质的可分泌性。模拟结果显示结构融合度特征能有效区分枯草芽孢杆菌宿主的可分泌和不可分泌蛋白。研究结果有助于信号肽的选择，对目的蛋白分泌表达的优化具有一定的指导意义。
|
| 关 键 词： | 信号肽，蛋白质分泌，结构融合度，特征提取 |
| 收稿时间： | 2009/11/19 0:00:00 |
Characterization of protein secretion based on structural fusion degree |
| |
| Cuifang Gao,Xiaojun Wu,Fengwei Tian,Yu Xia and Wei Chen.Characterization of protein secretion based on structural fusion degree[J].Chinese Journal of Biotechnology,2010,26(5):687-695. |
| |
| Authors: | Cuifang Gao Xiaojun Wu Fengwei Tian Yu Xia and Wei Chen |
| |
| Institution: | School of Information Engineering, Jiangnan University, Wuxi 214122, China;School of Information Engineering, Jiangnan University, Wuxi 214122, China;State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China;State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China;State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China |
| |
| Abstract: | Selection of suitable signal peptides is an important factor for efficient secretion of heterologous proteins. We defined structural fusion degree (SFD) as the compatibility degree of target proteins and signal peptides by a bioinformatics approach. We mathematically analyzed the interaction of fused signal peptides and adjacent residues of proteins, and proposed a mathematical model of extended signal region and the protein. SFD Features was extracted from this model to characterize the secretability of heterologous proteins. Simulation tests showed that SFD features can effectively discriminate high secretory proteins from poor ones in the host Bacillus subtilis. Results from this research will be useful in signal peptide selection and have a better guiding significance for the optimization of heterologous protein secretion. |
| |
| Keywords: | signal peptide secretion of protein structural fusion degree feature extraction |
| 本文献已被 CNKI 万方数据 等数据库收录！ |
| 点击此处可从《生物工程学报》浏览原始摘要信息 |
| 点击此处可从《生物工程学报》下载免费的PDF全文 |
|
