Discover the Post‐Translational Modification Proteome Using Mass Spectrometry

Abstract

Protein post‐translational modifications (PTMs) are chemical modifications on proteins. PTMs play a key role in many cellular processes by influencing the structure of proteins and dynamically regulating their functions. Therefore, characterizing PTMs at proteome level is critical to provide invaluable insight into the functions of proteins underlying different biological processes. Advances in modern proteomics technologies including sample preparation, chromatography separation as well as mass spectrometry have propelled the PTMs proteome to further depths. During the past decade, to better examine the PTMs with high sensitivity and selectivity, our group have developed a series of MS‐based novel analytical approaches to study the protein PTMs. Herein, we mainly introduce these approaches developed by our group and discuss how to overcome the technical obstacles of studying various protein PTMs with mass spectrometry. What is the most favorite and original method developed in your research group? The qualitative and quantitative approaches developed for analysis of PTM proteome. How do you get into this specific field? Could you please share some experiences with our readers? I entered Fudan University in 2003, when the sequencing of human genome was just completed. At that time, the life science entered the post‐genomic era, the era of proteomics. My post‐doctoral work is mainly based on mass spectrometry analysis, which is the core tool for proteome research. Therefore, I began to develop mass spectrometry‐based method for proteome research since then. What is the most important personality for scientific research? Creative, persistence, and collaboration. What's your hobbies? Playing badminton.

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