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作 者:赵小峰[1]
机构地区:[1]徐州医学院医学生物化学与分子生物学教学实验中心,江苏徐州221004
出 处:《生物技术》2015年第6期552-557,共6页Biotechnology
摘 要:[目的]对人VASH_1蛋白结构和功能进行生物信息学分析。[方法]利用生物信息学工具对人VASH_1蛋白的基因结构、跨膜区域、空间结构、理化性质和功能区进行预测。[结果]人VASH_1蛋白由365个氨基酸残基组成,该蛋白等电点9.50,相对分子质量40 956.5Da,分子式为C1805H2874N532O536S11。通过分析发现该蛋白为非跨膜的亲水蛋白,主要由无规卷曲构成。[结论]人VASH_1蛋白是由365个氨基酸残基组成的亲水蛋白,含有21个磷酸化位点和13个可能的抗原位点,与多种蛋白间存在相互作用。[ Objective]To predict the structure and function of human VASH1 protein with bioinformatics. [ Methods] The bioinformatie tools were used to predict the gene location, transmembrane region, spatial structure, the physical and chemical properties and functional category of VASH1 protein. [ Results] The bioinformatic analysis revealed that human VASHI protein contains 365 amino acid residues,the molecular formula was C1805H2274N532O536S11 with a relative molecular mass about 40. 957 kDa and PI 9.50. It is obtained that VASHl was a hydrophilie and non - transmembrane protein, its main component was ran- dom coil. [ Conclusion] The human VASH1 is a hydrophilie protein contains 365 amino acid residues,there are 21 phosphorylation sites and 13 epitopes bit in the human VASH1 protein sequence. There are several proteins directly interacting with VASHl.
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