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中文摘要：
磷酸化修饰是蛋白或多肽调节一种重要方法.利用分子动力学模拟方法,比较研究了蛋白激酶（protein kinase C-θ,PKCθ）催化域的转折片段Ser676位点磷酸化修饰前后的结构动力学特点.模拟结果和氢键分析显示,此位点的磷酸化修饰对这一片段的结构有显著的影响,有助于增加结构的稳定性.此结果有益于进一步研究PKCθ的结构动力学和相关实验研究.
英文摘要：
The phosphorylation is one of the most important method to modify the function or structure of the proteins and peptides. With molecular dynamic simulation, structural dynamics of the turn motifs in the catalytic domain of the protein kinase C-theta （PKCθ） for the phosphorylated and unphosphorylated Set 676 were compared. The simulation was analyzed to structural parameters hint the phosphorylation of this peptide stabilize its structure.
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