【摘要】 为了研究黄鳝(Monopterus albus)热休克蛋白70(Heat Shock Protein 70,简称HSP70)的结构和功能，试验采用生物信息学方法对黄鳝HSP70的基本理化性质、亲/疏水性、信号肽、磷酸化位点、糖基化、无序化特征、二级结构、三级结构、相互作用蛋白网络及进化树进行了研究。结果表明，黄鳝HSP70由441个氨基酸组成，相对分子质量为48146.31,等电点为5.98,整体呈碱性，是较稳定的亲水性蛋白质，有信号肽，但不存在跨膜结构，属于分泌型蛋白质。黄鳝HSP70存在35个潜在磷酸化位点，其中包括19个Ser、14个Thr和2个Tyr磷酸化位点，有5个典型的N糖基化位点。二级结构以α-螺旋(39.68%)、延伸链(20.41%)、β-折叠(6.58%)和无规则卷曲(33.33%)为主要结构。热休克蛋白70(HSP70)作为分子伴侣，在蛋白质折叠和运输、细胞周期调控、细胞凋亡和精子发生等方面发挥着重要作用。研究表明，黄鳝HSP70在抵抗外界应激源、环境应激保护等方面起着重要作用。更多还原

【Abstract】 In order to study the structure and function of Monopterus albus Heat Shock Protein 70(HSP70), bioinformatics methods were used to study the basic physical and chemical properties, hydrophilicity/hydrophobicity, signal peptides, phosphorylation sites, glycosylation, disorder characteristics, secondary structure, tertiary structure, interaction protein network and evolutionary tree of Monopterus albus Hsp70. The results showed that Monopterus albus HSP70 was composed of 441 amino acids, with a relative molecular weight of 48146.31 and an isoelectric point of 5.98. It was an alkaline, relatively stable hydrophilic protein with signal peptides, but no transmembrane structure, belonging to a secretory protein. There are 35 potential phosphorylation sites in Monopterus albus HSP70, including 19 ser, 14 thr and 2 Tyr phosphorylation sites, and 5 typical N-glycosylation sites. Secondary structure with α-Spiral(39.68%), extended chain(20.41%) β-Folding(6.58%) and irregular curling(33.33%) are the main structures. As a molecular chaperone, Heat Shock Protein 70(HSP70) plays an important role in protein folding and transport, cell cycle regulation, apoptosis and spermatogenesis. These results indicate that eel HSP70 plays an important role in resisting external stressors and protecting environmental stress.更多还原