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
出处
《应用与环境生物学报》
CAS
CSCD
北大核心
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~~
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
pathogenesis-related protein
molecular dynamics
homology modeling
fluorescence emitting spectra
thermal stability
