中文摘要：

蛋白质的三维结构在很多情况下不能很好地解释其在生理过程中的作用机制．动力学研究能够获悉蛋白质在不同时间尺度下的内运动信息，建立起动态结构和生物功能的联系．该文综述了通过NMR自旋弛豫技术研究蛋白质动力学的原理和方法：ps～ns的快运动分析主要采用约化谱密度函数映射和Modelfree方法；us～ms的慢运动涉及化学／构象交换过程，常借助CPMG和R1ρ弛豫色散手段．基于NMR的蛋白质动力学研究，将蛋白质科学从三维空间结构推进到四维时空结构的新层面．

英文摘要：

A static three-dimensional structure alone does not fully interpret the physiological functions of a protein in many cases. Dynamics studies can disclose internal motions of a protein on different time scales, providing a better link between dynamic structures and biological functions. In this review, the theoretical and experimental methods for protein dynamics studied by NMR spin relaxation are summarized. The reduced spectral density mapping and the Modelfree formulism are employed to describe fast motions on the ps-ns time scale. Slow motions on the us-ms time scale, associated with conformational and chemical exchanges, are often analyzed by CPMG and R1ρ relaxation dispersion curves. NMR-based dynamics studies promote protein structures from the three-dimensional date to the four-dimensional era.