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以螺旋结构的形成过程为研究对象,基于粗粒化的格子模型和动态蒙特卡罗模拟方法,初步探讨了非天然氢键相互作用对均聚多肽链螺旋折叠动力学过程的影响.研究发现,非天然氢键的引入虽然延缓了其热力学转变的发生,但也从整体上降低了折叠动力学过程的能垒,在某一特定温度之下,反而可以提高折叠速率.对其折叠路径分布的分析表明,非天然氢键可以减少慢速折叠路径的发生,而后者是导致折叠时间增加的主要因素.另一方面,比较特定温度下多肽链链构象及螺旋片断随时间的演化进程,发现非天然氢键在一定程度上影响了天然氢键的形成以及天然态构象的稳定存在,同时也加快了其部分解折叠过程.这说明,非天然相互作用的存在有利于蛋白质构象的快速动态调整,从而行使其相应的生物功能.
Based on the coarse-grained lattice model and dynamic Monte-Carlo simulation method, the influence of non-natural hydrogen bonding interaction on helical folding kinetics of Homopolymer peptides was investigated by using the formation process of helical structure as the research object. Although introduction of non-natural hydrogen bonds retards its thermodynamic transformation, it also reduces the energy barrier of the folding kinetic process as a whole, but increases the folding rate under a certain temperature instead. The analysis shows that the non-natural hydrogen bonding can reduce the occurrence of slow folding pathways, and the latter is the main factor leading to the increase of folding time.On the other hand, comparing the evolution of the peptide chain conformation and the helices with time at specific temperature, Natural hydrogen bonding to some extent affected the formation of natural hydrogen bonds and the steady state of natural state conformation, and also accelerated its partial unfolding process, indicating that the existence of non-natural interactions favors the rapid dynamic adjustment of protein conformation, Thus exercising its corresponding biological function.