论文部分内容阅读
采用简化的NHP模型并考虑蛋白质链的二级结构信息,对全α型蛋白质链进行构建.利用分子动力学模拟研究全α蛋白质体系势能的变化情况,得出键伸缩和弯曲能量随蛋白质的链长线性增加;单键的伸缩能和弯曲能随着温度的升高而线性增加,且伸缩能比弯曲能随温度的增加更为明显的结论.键扭转能随二级结构α螺旋数目的增加而线性降低,随温度的上升,扭转能变化呈现先增加后减少的趋势.非键能的大小随疏水残基在蛋白质组分中的比例增加而降低,但线性关系不明显.键扭转能和非键能都存在转变温度.蛋白质链的结构是由多种势能协同作用的结果,键能和非键能的相互竞争以及组成蛋白质链的氨基酸亲疏水性和二级结构组分都会影响蛋白质体系的能量,这些结果对深入理解蛋白质的结构提供理论依据.
Using a simplified NHP model and taking into account the secondary structure information of the protein chain, the full α-type protein chain was constructed.Using molecular dynamics simulation to study the changes of the potential energy of the whole α-protein system, we obtained the relationship between the bond stretching and bending energy with the protein chain The linear expansion of the single bond and the increase of the bending energy with the increase of the temperature are more obvious than the increase of the temperature with the increase of the bending energy.With the increase of the number of α helices of the secondary structure But decreased linearly with the increase of temperature, the twisting energy showed a trend of first increase and then decrease.The non-bond energy decreased with the increase of the proportion of hydrophobic residues in the protein components, but the linearity was not obvious.The bond twisting energy and Non-key energy exists in the transition temperature.The structure of the protein chain is the result of the synergy of multiple potential energy, the competing key energy and non-key energy, as well as the aminohydrophilic and secondary structural components of the protein chain all affect the protein system Energy, these results provide a theoretical basis for in-depth understanding of the protein structure.