【摘要】 为研究草地贪夜蛾（Spodoptera frugiperda）热休克蛋白Hsp70的功能，对Hsp70的理化性质、亲水/疏水性、二级结构、三级结构、跨膜结构及同源性等进行了分析和预测。结果表明，Hsp70基因共编码651个氨基酸，是稳定亲水蛋白，蛋白质二级结构主要为α-螺旋，其次为延伸链和无规则卷曲。Hsp70蛋白不具有信号肽及跨膜结构，与其他16种昆虫Hsp70蛋白的氨基酸序列进行对比，发现草地贪夜蛾的Hsp70蛋白与鳞翅目昆虫甜菜夜蛾（Spodoptera exigua）和斜纹夜蛾（Spodoptera litura）的亲缘关系较近。更多还原

【Abstract】 To investigate the function of Hsp70,the physical and chemical properties,hydrophilicity/hydrophobicity,secondary structure,tertiary structure,transmembrane structure,and homology alignment of Hsp70 were predicted and analyzed. The results showed that Hsp70 gene encoded 651 amino acids which was a stable hydrophilic protein. The secondary structure of the protein mainly consisted of α-Helix,followed by extended chains and random coils. The Hsp70 protein had no signal peptide and transmembrane structure.Compared with the Hsp70 proteins of 16 other insects,it was found that the Hsp70 protein of Spodoptera frugiperda was closely related to the Lepidoptera Spodoptera exigua and Spodoptera litura.更多还原