Identification of Two Novel Modifications at Tryptophan Residues

Shuzhen Zheng; Kai Zhang; Shanshan Tian; Xiwen He; Yukui Zhang

doi:10.1007/s13361-015-1217-8

Identification of Two Novel Modifications at Tryptophan Residues

J Am Soc Mass Spectrom. 2015 Oct;26(10):1787-90. doi: 10.1007/s13361-015-1217-8. Epub 2015 Aug 4.

Authors

Shuzhen Zheng¹, Kai Zhang^{2

3}, Shanshan Tian⁴, Xiwen He¹, Yukui Zhang^{5

6}

Affiliations

¹ Department of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China.
² Department of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China. zhangkai@nankai.edu.cn.
³ Department of Biochemistry and Molecular Biology & Tianjin Key Laboratory of Medical Epigenetics, Tianjin Medical University, Tianjin, 300070, People's Republic of China. zhangkai@nankai.edu.cn.
⁴ Department of Biochemistry and Molecular Biology & Tianjin Key Laboratory of Medical Epigenetics, Tianjin Medical University, Tianjin, 300070, People's Republic of China.
⁵ Department of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China. ykzhang@dicp.ac.cn.
⁶ National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, People's Republic of China. ykzhang@dicp.ac.cn.

PMID: 26238325
DOI: 10.1007/s13361-015-1217-8

Abstract

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 + 92 Da and W + 108 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.

Keywords: Mass spectrometry; Post-translational modifications; Proteomics; Tryptophan modifications.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Protein Processing, Post-Translational*
Proteomics
Tandem Mass Spectrometry / methods*
Tryptophan / analysis
Tryptophan / chemistry*

Substances

Tryptophan