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The research group of Professor Lei Xiaoguang and Professor Tang Chun of the School of Chemistry and Molecular Engineering of Peking University cooperated with the research group of Professor Dong Mengqiu of the Beijing Institute of Biological Sciences to publish a collaborative paper in the journal Nature Communications with the title " Characterization of protein unfolding by fast cross- linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers ”
Chemical cross-linking coupled with mass spectrometry (CXMS) is a method that has developed rapidly in recent years to detect protein structure and protein interactions
Based on this, in order to further enrich the types of cross-linking agents, researchers developed a series of lysine-selective cross-linking agents based on ortho-phthalaldehyde structure, named DOPA, which can effectively link There are two lysine residues on the surface of the protein (Figure 1)
Figure 1.
Figure 2.
When the researchers further explored the properties of DOPA cross-linking agent, they found that DOPA cross-linking agent exhibited the characteristics of non-hydrolysis, fast reaction speed, low temperature resistance, low pH and denaturant, so they decided to apply it in the process of protein denaturation and unfolding.
Figure 3.
Lei Xiaoguang, Dong Mengqiu and Tang Chun are the co-corresponding authors of the paper
