波谱学杂志 ›› 2004, Vol. 21 ›› Issue (4): 385-396.

• 研究论文 •    下一篇

用异核多维NMR技术研究蛋白质动力学

廖新丽2,  林东海1   

  1. 1.中国科学院 上海药物研究所,上海生命科学研究院,上海 201203; 2.厦门大学 化学系, 福建 厦门 361005
  • 收稿日期:2004-03-29 修回日期:2004-08-26 出版日期:2004-12-05 发布日期:2004-12-05
  • 基金资助:

    中国科学院“百人计划”研究基金、上海市重点基础研究基金(03JC14081)和厦门大学预研基金资助项目.

PROTEIN DYNAMICS STUDIED BY HETERONUCLEAR MULTI-DIMENSIONAL NMR

 LIAO Xin-Li2, Lin-Dong-Hai1   

  1. 1.Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China;
    2.Department of Chemistry, Xiamen University, Xiamen 361005, China
  • Received:2004-03-29 Revised:2004-08-26 Online:2004-12-05 Published:2004-12-05
  • Supported by:

    中国科学院“百人计划”研究基金、上海市重点基础研究基金(03JC14081)和厦门大学预研基金资助项目.

摘要:

蛋白质在溶液中的三维空间结构、动力学与蛋白质生物功能的关系是在分子水平上理解生命现象的重要基础. NMR技术在研究蛋白质动力学方面具有独特的优势,所能表征的运动过程相关时间尺度很广. 文章综述了异核多维NMR技术研究蛋白质动力学的实验技术和理论方法,介绍了描述蛋白质动力学的内运动参量的意义和Model-Free 方法,并举例说明15N弛豫测量实验被用于研究蛋白质及其与配体复合物的动力学. 

关键词: 异核多维核磁共振, 蛋白质, 动力学, 内运动, 构象交换

Abstract:

One of the fundamental problems in understanding life science at the molecular level is the relationship among structure, dynamics, and function of proteins. NMR has a unique capacity to investigate dynamics properties of proteins over a range of different time scales with atomic resolution. This review focuses on the experimental and theoretical methods used in heteronuclear spin relaxation measurement for studying protein dynamics, and the parameters describing the protein internal motion as well as the Model-Free method. Finally, some application examples are given in which 15N relaxation measurements were performed to study the backbone dynamics of protein and protein-ligand complex.

Key words: protein, relaxation, dynamics, mobility, heteronuclear NMR

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