Bioinformatics analysis of heat-shock protein Hsp70 from Spodoptera frugiperda

doi:10.14088/j.cnki.issn0439-8114.2022.24.033

Abstract

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.

Key words: Spodoptera frugiperda, heat-shock proteins, environmental stresses, bioinformatics

CLC Number:

S433.4

LIU Fang, ZHANG Zhi-gang, FANG Wei, WANG Kai-mei, WANG Yue-ying. Bioinformatics analysis of heat-shock protein Hsp70 from Spodoptera frugiperda[J]. HUBEI AGRICULTURAL SCIENCES, 2022, 61(24): 153-159.

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