Analytical Techniques for Phosphoproteomics

Abstract

Phosphorylation, one of the post-translational modifications of the protein, confers negative charge and hydrophilicity to specific amino acids, affecting protein function by changing its conformational state, stability, or interactions with other molecules. Protein phosphorylation therefore plays an important role as a regulatory mechanism in a wide variety of biological processes. To accurately understand protein function, phosphoproteomics must not only identify modification sites, but also reveal all the details through quantitative and qualitative analysis of phosphoproteins. In recent years, various analytical strategies have been proposed for analyzing the phosphorylation status of proteins, facilitating the analysis of a very large number of phosphoproteins. Here, powerful analytical techniques for phosphoproteomics based on electrophoresis and mass spectrometry will be introduced, with a focus on ‘Phos-tag’. We believe that these analytical techniques will help accelerate our understanding of protein function involved in biological processes.