Protein Ubiquitination Sites Identification by Mass Spectrometry

Ubiquitination modification is an important post-transcriptional modification of proteins in living organisms, with profound effects on many physiological processes such as gene expression, cell cycle regulation, and immune responses. However, the accurate identification of ubiquitination sites and their specific biological significance is one of the frontier challenges in the field of biopharmaceuticals.

 

The Advantages of Mass Spectrometry

Mass spectrometry, as a new analytical technique, has a natural advantage in unraveling and analysing the complex protein modification network in living organisms. It can not only identify the types of proteins, but also accurately point out the modification sites, providing the possibility for us to deeply understand the working mechanism of ubiquitination modification.

 

The Key to Mass Spectrometry Judging Protein Ubiquitination

Accurate mass spectrometry identification requires suitable reagents and precise experimental operations. To use mass spectrometry for qualitative analysis, we need to design a specific labelling strategy. This is because in the process of ubiquitination, the unique modification form left behind by the ubiquitination site is crucial for accurately judging whether a protein has been ubiquitinated.

 

The Biological Significance of Ubiquitination Modification

Scientists have found that ubiquitination modification usually accompanies changes in protein function. Ubiquitinated proteins may change their location or even lose their function. Therefore, understanding the ubiquitination site can help us reveal the key role of ubiquitination modification in biological processes.