Development of analytical method for structural change dynamics of biomolecules and its application

犬乳溶菌酶（CML）是一种钙结合蛋白，属于溶菌酶家族。尽管CML与山羊α-乳白蛋白（GLA）高度同源，但近年来的实验结果发现CML的去折叠途径与GLA不同。我们通过全原子分子动力学模拟研究了CML和GLA的去折叠途径之间的差异。因此，我们发现解折叠途径的差异是由于这些蛋白质中存在或不存在局部相互作用。此外，我们还发展了一种基于三阶非线性光谱的结构跃迁分析方法。

Canine milk lysozyme (CML) is a calcium binding protein belonging to the lysozyme family. Although CML and goat α-lactalbumin (GLA) are highly homologous, it was found in recent experimental results that the unfolding pathway of CML is different from that of GLA. We examined the difference between the unfolding pathways of CML and GLA by performing all-atom molecular dynamics simulations. As a result, we found that the difference of the unfolding pathways is due to the presence of absence of local interactions in these proteins. In addition, we developed a novel method for the structure transitions based on third-order nonlinear spectroscopy.