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分子模拟为从微观角度理解生物大分子提供了有利的工具。本文采用分子动力学方法研究在Pt(100)、Pt(110)及Pt (111)三种晶格界面上聚十赖氨酸分子的吸附,以从分子水平上研究蛋白质吸附的动态过程和机理。界面的作用使部分聚十赖氨酸分子出现了较明显的二面角变化,说明吸附过程中界面的特性对聚赖氨酸的分子结构有影响;在Pt(100)与Pt(111)界面上,聚十赖氨酸分子构象变化较大,Pt(110)变化较小。聚十赖氨酸分子在吸附中,能量变化与分子构象变化的结果一致,构象变化较大的Pt(100)和Pt(111)界面上聚十赖氨酸分子能量的平均值高于Pt(110)。聚十赖氨酸分子在Pt(100)与Pt(111)界面上先远离界面运动,然后在某位置稳定波动;在Pt(110)界面上先靠近界面运动一段时间后又远离界面。
Molecular modeling provides an advantageous tool for understanding biological macromolecules from a microscopic point of view. In this paper, we study the adsorption of poly-10-lysine on Pt (100), Pt (110) and Pt (111) lattice interfaces with molecular dynamics method to study the dynamic process and mechanism of protein adsorption . The interaction of poly (L-lysine) and poly (L-lysine) on the interface of Pt (100) and Pt (111) shows that the characteristic of interfacial adhesion has an influence on the molecular structure of polylysine. On the other hand, the molecular structure of poly-10-lysine changed a lot and the change of Pt (110) was smaller. The results showed that the energy change of poly-10-lysine molecule was consistent with the change of molecular conformation. The average energy of poly-10-lysine molecule at Pt (100) and Pt (111) 110). Poly-10-lysine molecules first moved away from the interface at the Pt (100) and Pt (111) interfaces and then stably fluctuated at a certain position; on the Pt (110) interface, it was first moved away from the interface after moving towards the interface for some time.