结构和动力学是蛋白质发挥功能的基础。核磁共振是在原子层次研究蛋白质结构和动力学的主要手段之一，已被广泛应用于研究天然蛋白质。由于计算方法发展，人工设计的蛋白也可以具有与天然蛋白类似的稳定结构和相互作用等功能，但它们往往表现出与天然蛋白截然不同的动力学特性。用核磁共振分析人工设计蛋白，可以从新的视角来分析蛋白质结构、动力学和功能关系；通过与天然蛋白对照，可探索进化在蛋白质获得其动力学特性中的作用。此前，我们成功设计了若干具有稳定结构以及具有蛋白-蛋白相互作用功能的人工蛋白。在此基础上，我们将通过序列重设计、定向进化等获得具有不同结构稳定性、不同相互作用强度的人工蛋白，用核磁共振全面表征它们原子层次的结构和动力学，分析其与序列和相互作用的关系，并与相应天然蛋白比较，由此对动力学在蛋白质结构功能及其进化中的作用获得更全面的认识，并为相互作用等功能蛋白质的设计、定向进化等提供指导。

Structure and dynamics are fundamental to protein functions. Nuclear magnetic resonance (NMR) is one of the primary techniques to investigate protein structure and dynamics at the atomic level and has been widely used in studies of natural proteins. With the development of computational methods, de novo designed proteins show stable structures and interactions similar to natural proteins, while tend to exhibit distinct kinetic properties. Characterization of these designed proteins with NMR means may help us to understand protein structure-functional relationship from a new perspective. By comparison with natural proteins, we could explore how evolution affects protein dynamics during natural selection. We have successfully designed a number of proteins with stable structures and protein-protein interactions. Based on these previous work, we will acquire more artificial proteins with different structural stability and interaction affinity through sequence design and directional evolution. We will characterize their atomic-level structures and dynamics in detail with NMR to explore the relationships between sequence and function in comparisons with natural proteins. This study can provide a more comprehensive understanding of the role of protein dynamics in structure, function and evolution, which can guide functional protein design and directed evolution.