摘要
本研究应用相关生物学软件和在线数据库对大肠杆菌的HspQ基因进行生物信息学分析。结果表明其编码了105个氨基酸,推测其可能是一种亲水性蛋白,而通过蛋白磷酸化位点的预测表明其含有17个丝氨酸位点、7个苏氨酸位点、4个酪氨酸位点,通过对其跨膜结构域和信号肽预测显示其不存在信号肽也没有跨膜结构域。而我们对其编码蛋白的二、三级结构进行预测表明其主要由α螺旋和无规则卷曲两种结构组成。本研究预测结果为进一步研究热休克蛋白基因奠定了基础。
Bioinformatics analysis of the Escherichia coli HspQ gene was performed using biological software and related databasesin in this study. The results showed that it encodes 105 amino acids and it is speculated that it may be a hydrophilic protein. The prediction of protein phosphorylation sites shows that it contains 17 serine sites, seven threonine sites and four tyrosine acid sites.It is shown by the prediction of its transmembrane domain that this gene may have signal peptide but no transmembrane domain.The prediction of the second and third order structure of its encoded protein indicates that it mainly contains two kinds of structures： α-helix and random-curl. This study laid the foundation for the further study of the heat shock protein gene.
作者
周辉
宋莉
赵德刚
ZHOU Hui;SONG Li;ZHAO De-gang(Guizhou Key Lab of Agro-Bioengineering,Institute of Agro-Bioengineering and College of Life Sciences,Guizhou University,Guiyang,Guizhou 550025,China;Guizhou Academy of Agricultural Science,Guiyang,Guizhou 550006,China)
出处
《山地农业生物学报》
2018年第5期57-61,共5页
Journal of Mountain Agriculture and Biology
基金
贵州省优秀科技教育人才省长基金项目(黔省专合字[2012]59号)资助
