Chinese Journal of Magnetic Resonance ›› 2005, Vol. 22 ›› Issue (1): 85-98.

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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.

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

CLC Number: