Identification of Two Novel Modifications at Tryptophan Residues

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• 作者：Shuzhen Zheng ; Kai Zhang ; Shanshan Tian…
• 关键词：Proteomics ; Mass spectrometry ; Post ; translational modifications ; Tryptophan modifications
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2015
• 出版时间：October 2015
• 年：2015
• 卷：26
• 期：10
• 页码：1787-1790
• 全文大小：600 KB
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• 作者单位：Shuzhen Zheng (1)
  Kai Zhang (1) (2)
  Shanshan Tian (2)
  Xiwen He (1)
  Yukui Zhang (1) (3)
  
  1. Department of Chemistry, Nankai University, Tianjin, 300071, People’s Republic of China
  2. Department of Biochemistry and Molecular Biology & Tianjin Key Laboratory of Medical Epigenetics, Tianjin Medical University, Tianjin, 300070, People’s Republic of China
  3. National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, People’s Republic of China
  
• 刊物主题：Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
• 出版者：Springer US
• ISSN：1879-1123

文摘

Protein post-translational modifications (PTMs) play important roles in cellular physiology. Mass spectrometry (MS) has been developed into a powerful tool to identify all possible protein modifications. Herein, we describe our efforts to deduce the structures of two unknown modifications at tryptophan (Trp) residues (W--2 Da and W--08 Da). The two modifications were further confirmed by aligning the MS/MS fragmentation of synthetic peptide with in-vivo peptide identified. Finally, the mimic experiment elucidated how two Trp modifications occur. This study, therefore, expands current knowledge of Trp modifications.