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不同亚型乙肝病毒Pre-S(2)蛋白二级结构及抗原表位的预测与比较
引用本文:吳玉章,朱锡华.不同亚型乙肝病毒Pre-S(2)蛋白二级结构及抗原表位的预测与比较[J].中国生物化学与分子生物学报,1993,9(2):229-233.
作者姓名:吳玉章  朱锡华
作者单位:第三军医大学免疫学教研室,第三军医大学免疫学教研室 重庆 630038,重庆 630038
摘    要:本文采用Chou和Fasman方法预测adw,adr,ayw三种亚型的乙肝病毒Pres(2)蛋白的二级结构;并用双亲性方案和亲水性方案分析了抗原表位。结果显示三者均可能含有较多的β片层和β转折;N-末端30个残基所形成的二级结构较保守,而C-末端顺序的构象在亚型间差别较大;Th细胞识别的表位可能在39—49肽段;B细胞识别的表位可能主要在12—18残基或其附近。

关 键 词:预测二级结构  双亲性  亲水性  表位  
收稿时间:1993-04-20

Prediction and Comparison of the Secondary Structures and Epitopes for Pre-S (2) Region of Different Subtype HBV
Wu,Yu-zhang Zhu,Xi-hua.Prediction and Comparison of the Secondary Structures and Epitopes for Pre-S (2) Region of Different Subtype HBV[J].Chinese Journal of Biochemistry and Molecular Biology,1993,9(2):229-233.
Authors:Wu  Yu-zhang Zhu  Xi-hua
Institution:(Department of Immunology,The Third Medical University of The Army, Chongqing 630038
Abstract:The secondary structures of pre-s(2) region of adw, adr, ayw subtype HBV were predicted by Chou and Fasman's method, and the antigenic epitopes were analysed by using amphipathic plot and hydrophilicity plot. The results showed that all the three subtypes are rich in β-turns; the conformation of the N-terminal sequence is highly conserved, but of the C-terminal sequence is of polymorphism; the epitope recognized by Th cells may be at 39—49, and by B cells at or adjacent to 13—18.
Keywords:Secondary structure predietion  Epitope  Amphipathic structures  Hydrophilicity  
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