紫花苜蓿乙酰CoA硫解酶的生物信息学分析与同源建模

目的]对紫花苜蓿中的乙酰CoA硫解酶进行生物信息学分析与同源建模。方法]应用生物信息学软件预测紫花苜蓿乙酰CoA硫解酶的理化性质、亲/疏水性、卷曲螺旋结构、糖基化位点、活性位点、亚细胞定位、二级结构、结构域及三维高级结构。结果]该蛋白质是一个极疏水性蛋白,含403个氨基酸,理论等电点为6.95;包含1个明显卷曲螺旋结构、5个糖基化位点、1个硫解酶结构域;二级结构中α-helix(Hh)占39.95%、Extended strand(Ee)占16.38%、Random coil(Cc)占43.67%;Ramachandram结构检测表明预测蛋白质残基的二面角有90%以上位于黄色区域,符合立体化学能量规则。结论]为该蛋白功能的探索提供了一定的理论参考。

Bioinformatics Analysis and Homology Modeling of Acetoacetyl-CoA thiolase(mAACT) from Medicago sativa L.

Objective] Bioinformatics analysis and homology modeling were carried out on Acetoacetyl-CoA in Medicago sativa.Method] According to the mRNA and amino acid sequence,the character of mAACT(Acetoacetyl-CoA thiolase) such as the physical and chemical properties,hydrophilicity/hydrophobicity,coiled coil,O-glycogylation site,active site,subcelluar localization,Secondary structure,functional structural domains and three-dimensional structure were analyzed by a series of bioinformatics software.Result] The results showed that mAACT was a hydrophobic highly and stable protein with 5 O-glycogylation sites,1 coiled coils distinctly.It has 403 amino acids,the theoretical pI is 6.95.In the secondary structure,α-helix,Extended strand,random coil is 39.95%,16.38%,43.67% respectively.The diagram of Ramachandram showed that the validation of modeling as more than 90% dihedral angel of protein residue located in yellow region accords with the stereochemistry.Conclusion] To provide theoretical reference for exploration of protein function.