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目的:研究氨基酸的带电量及分布对蛋白质单链自组装行为的影响。方法:利用LAMMPS软件构建不同带电量及电荷分布的蛋白质模型，采用分子动力学对体系进行模拟。结果:体系静电势能和范德华能随氨基酸带电荷情况(带电荷量与同极性带电荷氨基酸连续数目)呈相反的变化趋势，体系静电势能绝对值远大于键能和范德华能，并且总势能的变化趋势与静电势能变化趋势一致，说明静电相互作用在非键相互作用中起主导作用。从模型的回转半径分析易得同极性电荷氨基酸连续数较小时，蛋白质结构的松散程度与单个氨基酸带电荷量大小呈正相关。结论:组成蛋白质氨基酸的带电量和电荷分布体现了静电相互作用强度及连续性，它们对蛋白质链的结构都有直接影响。这些研究成果为更好地理解蛋白质在不同静电作用下的结构特征及转变行为提供了理论依据。
Abstract：Aims: This paper aims to study the effect of the charge and its distribution of amino acids on the single chain self-assembly behavior of proteins. Methods: The protein models with different charge and charge distribution were constructed by LAMMPS software; and the system was simulated by molecular dynamics. Results: The electrostatic potential energy and van der Waals of the system had opposite changing trends with the charge of amino acids(the amount of charge and the continuous number of amino acids with the same polarity of charge). The absolute value of the electrostatic potential energy of the system was much greater than the bond energy and van der Waals energy; and the changing trend of the total potential energy was consistent with that of the electrostatic potential energy, indicating that the electrostatic interaction played a leading role in the non-bond interaction. From the analysis of the rotation radius of the model, it was easy to find that the continuity number of amino acids with the same polarity charge was small and the looseness of the protein structure was positively correlated with the charge amount of a single amino acid. Conclusions: The electric quantity and charge distribution of amino acids in proteins reflect the strength and continuity of electrostatic interaction, which have a direct impact on the structure of protein chains. These results provide a theoretical basis for better understanding the structural characteristics and transformation behavior of proteins under different electrostatic interactions.
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基本信息:
DOI：
中图分类号:O629.73
引用信息:
[1]俞志超,姜舟婷.氨基酸带电量及分布对蛋白质单链自组装行为的影响[J].中国计量大学学报,2023,34(03):478-484+494.
基金信息:
国家自然科学基金项目(No.21873087)