波谱学杂志 ›› 2012, Vol. 29 ›› Issue (2): 288-306.

• 综述评论 • 上一篇    

基于NMR自旋弛豫技术的蛋白质动力学研究

文祎1,林东海1,2*   

  1. 1. 中国科学院 上海药物研究所 生物核磁共振实验室,上海 201203;
    2. 厦门大学 化学化工学院 化学生物学系结构生物学实验室,福建 厦门 361005
  • 收稿日期:2011-05-16 修回日期:2011-06-15 出版日期:2012-06-05 发布日期:2012-06-05
  • 基金资助:

    国家自然科学基金资助项目(30730026,30570352);上海市优秀学科带头人计划资助项目(09XD1405100).

Protein Dynamics Studied by NMR Spin Relaxation

 WEN Yi1, LIN Dong-Hai1,2*   

  1. 1. Bio-NMR Laboratory, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China; 
    2. Laboratory of Structural Biology, Department of Chemical Biology, College of Chemistry & Chemical Engineering, Xiamen University, Xiamen 361005, China
  • Received:2011-05-16 Revised:2011-06-15 Online:2012-06-05 Published:2012-06-05
  • Supported by:

    国家自然科学基金资助项目(30730026,30570352);上海市优秀学科带头人计划资助项目(09XD1405100).

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;μs~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.

关键词: 核磁共振(NMR), 蛋白质, 动力学, 自旋弛豫

Abstract:

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 μs~ms time scale, associated with conformational and chemical exchanges, are often analyzed by CPMG and R  relaxation dispersion curves. NMR-based dynamics studies promote protein structures from the three-dimensional date to the fourdimensional era. 

Key words: NMR, protein, dynamics, spin relaxation

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