波谱学杂志 ›› 2005, Vol. 22 ›› Issue (1): 85-98.

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残留偶极耦合及其在蛋白质结构研究中的应用

  

  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.北京大学 天然药物及仿生药物国家重点实验室,北京 100083
  • 收稿日期:2004-03-22 修回日期:2004-08-30 出版日期:2005-03-05 发布日期:2005-03-05
  • 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)和上海市引进海外高层次留学人员专项资金资助项目.

Residual Dipolar Couplings and Their Applications in Determination of Protein Structures

  1. 1.Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203,China;
    2.National Lab of Natural and Biomimetic Drug, Peking University, Beijing 100083,China
  • Received:2004-03-22 Revised:2004-08-30 Online:2005-03-05 Published:2005-03-05
  • 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)和上海市引进海外高层次留学人员专项资金资助项目.

摘要:

近年来溶液中残留偶极耦合常数被用来获取生物大分子化学键之间相对取向等长程构象约束条件,用于计算或优化蛋白质及其复合物的三维空间结构. 介绍了用异核多维NMR技术测量残留偶极耦合常数的方法,及其在蛋白质结构计算中的一些应用:优化蛋白质溶液结构,评价蛋白质结构质量,确定蛋白质结构域取向,获取有关配体的构象和取向的信息,在缺乏NOE数据时构建蛋白质结构等. 

关键词: 核磁共振, 残留偶极耦合常数, 三维溶液结构, 蛋白质

Abstract:

In recent years residual dipolar couplings have been employed to obtain the long-range conformational constraints such as the relative orientations between the chemical bonds in biomolecules for calculation or refinement of three-dimensional structures of proteins and protein complexes in solution. This review describes the measurement of residual dipolar couplings using multi-dimensional NMR techniques and their applications in determination of protein structures: refining protein structures, evaluating protein structures, determining the relative orientation between protein domains, obtaining information about ligand conformation and orientation, etc.

Key words: NMR, residual dipolar couplings, 3D solution structures, proteins

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