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机构地区:[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,四川成都610064 [2]吉林大学理论化学研究所理论化学计算国家重点实验室,吉林长春130023
出 处:《应用与环境生物学报》2008年第4期466-468,共3页Chinese Journal of Applied and Environmental Biology
基 金:教育部新世纪人才资助计划(NCET-04-0861);四川大学985计划项目~~
摘 要:利用同源模建和分子动力学模拟方法搭建了烟草病程相关蛋白PR-1a的三维结构,在此基础上预测出PR-1a具有2个可能的活性位点,进一步分析PR-1家族特异保守序列,结果显示位点1的可能性更大.利用蛋白质内源荧光为探针,对分离的重组表达PR-1a蛋白进行了热稳定性研究.低于60℃处理,PR-1a蛋白内源荧光只略微降低;70℃处理30min引起PR-1a蛋白内源荧光明显降低,结果显示,PR-1a中色氨酸残基主要处于蛋白质分子内部,这与三维结构模型预测结果相符.Tobacco PR-1a model was obtained with the aid of the homology modeling and molecular dynamics methods, and was found reliable in Profile-3D and ProStat assessments. On the basis of this model, the omponents and structure of the active sites in tobacco PR-1a were analyzed. Further analysis of the conserved sequence in PR-1 family suggested that site 1 was likely more active than site 2. Then, fluorescence spectra were used as the probe to investigate the thermal stability of purified recombinant PR-1a proteins. The fluorescence intensity of PR-1a was reduced slightly when treated at 20-60 ℃, but it was obviously weakened at 70 ℃ for 30 minutes. The results indicated that tryptophan residues were mostly at the interior of PR-1a protein, which was consistent with the final 3D model. Fig 5, Ref 15
关 键 词:病程相关蛋白 分子动力学 同源模建 荧光发射光谱 热稳定性
分 类 号:S432.1[农业科学—植物病理学]
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