分析小鼠极光激酶A(Aurora-A)蛋白的性质和结构特征.利用NCBI、ExPASy和CBS网站中的各种生物信息学分析工具,对小鼠Aurora-A蛋白质的理化性质、亲疏水性、二/三级结构以及磷酸化和SUMO化位点进行分析.小鼠Aurora-A蛋白是一个不稳定的亲水性碱性蛋白质;二级结构中含有27.10%的α-螺旋、11.99%的延伸链、5.28%的β-转角和55.64%的无归卷曲;共含有43个磷酸化位点和一个保守的SUMO化序列.Aurora-A的蛋白质的性质和结构特征的分析为进一步研究其在生理和病理条件下的功能和调控机制提供实验依据.
To analyze the properties and structural characteristics of Aurora-A protein.NCBI,Expasy,and CBS websites were used to analyze the physicochemical property,hydrophilicity/hydrophobicity,secondary/tertiary structures,as well as phosphorylation and SUMOylation of mice Aurora-A protein.Aurora-A protein in mice was a unstable hydrophilic structural alkaline protein,which contained 28.10%of α-helics,6.33%β-turn and 52.66%random coil in its secondary structure.It had a total of 43 phosphorylation sites and a conservative SUMO sequence.The analysis of the properties and structural characteristics ofAurora-A protein provides experimental basis for further study of its functions and regulatory mechanisms under physiological and pathological conditions.