蛋白质大分子承担了生命体绝大多数的生物功能，然而这些功能的实现往往依赖于蛋白所处的水溶液环境。蛋白质表面的水分子的动力学对蛋白的结构稳定性，对接底物分子，结构相变（折叠/解折叠），低温动力学转变（蛋白在200K左右从柔软的功能态冻结到无功能固态的转变）等等都有重要意义。大多数谱学方法一般缺乏空间分辨率，这限制了对蛋白表面水分子微观动力学的时空间特征的定量表征。我们通过前期工作，摸索出经济高效的氘化蛋白的制备技术，并运用中子散射实验原位表征了该蛋白界面水分子的反常扩散行为。本项目将在前期工作的基础上，结合中子散射，氘化技术以及分子动力学模拟，深入研究蛋白质表面水分子微观动力学的时空间特征，以及水分子动力学在蛋白质高温解折叠和低温动力学转变过程中的作用机制。这些研究不仅有利于深入理解水分子的生物意义，也对设计耐高温工业酶和医用蛋白，以及开发新型生物低温保存技术有现实价值。

Proteins carry out most bio functions for our life. These functions are often realized with the protein molecules being present in the aqueous environment. The dynamics of protein-surface water plays an essential role in stabilizing the protein structure, mediating the docking of the proteins to small ligands and other bio macromolecules, facilitating the folding/unfolding of the native structures of the proteins, and driving the low-temperature dynamical transition of the protein molecules around 200 K from the flexible functional form to the rigid nonfunctional solids, etc. Most spectroscopic methods can only furnish the characteristic time scale for the dynamics of water molecules without providing the spatial resolution. This hinders the quantitative measurement of the temporospatial characteristics of the microscopic dynamics of water molecules on the protein surface. In the past, we have successfully synthesized fully deuterated proteins and performed neutron scattering experiments on these proteins to reveal the sub diffusive dynamics of the surface water molecules. Based on these preliminary work, the present project plans to combine neutron scattering, deuteration technique and molecular dynamics simulations together to study the temporospatial characteristics of the dynamics of the protein-surface water molecules and its temperature dependence. The goal is to reveal the microscopic role of the surface water molecules in the high-temperature unfolding and the low-temperature dynamical transition of the protein molecules. These studies will not only further the understanding of the biological significance of water, but also can facilitate the design of the thermophilic proteins for the industry and pharmaceutic applications, and the development of the advanced technique for bio preservation.