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Progress in Chemistry 2008, Vol. 20 Issue (06): 975-983 Previous Articles   Next Articles

• Review •

Protein Disulfide Bond Determination and Its Analysis by Mass Spectrometry

Qiu Xiaoyan1,2  Cui Meng1 Liu Zhiqiang1 Liu Shuying1**   

  1. (1. Changchun Center of Mass spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China; 2. Graduate School of the Chinese Academy of Sciences, Beijing 100039, China)
  • Received: Revised: Online: Published:
  • Contact: Shuying Liu
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Disulfide bonds are one of the most common covalent posttranslational modifications of proteins. They play an important role in maintaining the three-dimensional structures of proteins, and their biological activities. Therefore, the determination of disulfide bonds becomes an important aspect of obtaining a comprehensive understanding of the chemical structure of a protein. Numerous experimental methods have been developed for the determination of disulfide bonds in proteins. Modern mass spectrometry has developed as an important tool for the analysis of disulfide bond patterns due to its advantages of being simple, rapid and sensitive. Some useful methods for assignment of disulfide bonds in proteins are introduced, the developments and applications of mass spectrometry in this area are reviewed.

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