十二烷基硫酸钠（SDS）调控蛋白α-螺旋及聚集作用双重行为机制的研究以及复合物模型的构建对于更好理解蛋白质去折叠与重折叠过程及其机理、发展表面活性剂辅助蛋白质复性技术具有重要意义。本项目以SDS和球状蛋白为对象，一方面研究不同形态SDS（单分子及胶团）诱导蛋白质构象转变及复合物结构变化对体系热力学行为、界面特性及吸附模型的影响规律；建立分子间作用力与蛋白α-螺旋、复合物形态结构匹配性的能量构象关联，阐明SDS调控蛋白质去折叠及复性的驱动力和诱导取向；另一方面明确SDS与蛋白极性和电负性协同效应对聚集作用调节机制及介导因素，研究聚集体构成与胶团分布互控规律，揭示单体复合物与聚集体间双向转变的关键环节；基于SAXS构建熔融中间态蛋白修饰的类胶团核壳理论模型，明确复合物单体和聚集体的结构特征；旨在完善SDS调控蛋白α-螺旋及聚集作用双重行为机制理论框架，为表面活性剂辅助蛋白复性技术提供科学依据。

The research of dual behavior of the α-helix structure and aggregation of protein regulated by sodium dodecyl sulfate (SDS) and construction of complex's model is important for better understanding the process and mechanism of unfolding and refolding of protein, and also for the technology of surfactant-assisted renaturation of protein. In this project, we target SDS and globular protein, on the one hand, investigate the conformational transition of protein and changes of complexes' structure induced by different forms of SDS molecules (monomer and micelle), and its influence rule for the thermodynamics behavior, interface property and absorption model of system. Constructing the conformational energy relationship for matching of the intermolecular force, α-helix of protein and forms of complexes. Clarifying the driving force and induced orientation of the SDS-regulated unfolding and refolding of protein. On the other hand, defining the regulating mechanism of synergy of polarity and electronegativity of SDS and protein for aggregation and media factors, and investigating the mutual regulating rule between the component of aggregate and distribution of micelles, and revealing the key links of bilateral transformation between monomer complex and aggregate. Develop a model that molten globule state protein decorated micelle like core-shell structure for monomer complex and aggregate based on SAXS., and define the structural properties of monomeric complex and aggregate. The proposed project aims at improving the theoretical framework of mechanism of SDS-regulated dual behavior of α-helix and aggregation of protein, and providing the scientific evidence for the technology of surfactant-assisted renaturation of protein.