Post-Translational Modifications of Proteins

Many proteins undergo a covalent modification process during processing and synthesis, which involves changing the properties of the protein by adding functional groups at amino acid residues under the action of corresponding enzymes. This process is called post-translational modifications (PTMs). Currently, more than 400 different types of post-translational modifications have been discovered, with the main forms including glycosylation, phosphorylation, methylation, acetylation, ubiquitination, etc. Protein post-translational modifications have significant physiological significance and are involved in regulating various life activities, such as the physicochemical properties, active state, cellular localization, signal transduction, and protein-protein interactions.

Proteomics of protein post-translational modificationsMainly studies the types of protein post-translational modifications and the levels at which these modifications occur. Currently, commonly used methods for identifying protein post-translational modifications include electrophoresis, chromatography, and mass spectrometry. Due to the low levels of post-translational modifications, instability of the covalent bonds formed, insignificant differences before and after modification, diverse types, and possible simultaneous presence, identifying them is challenging. Therefore, enrichment and separation of modified proteins are crucial in research.

Biotechnology company Biotai Park providesproteinpost-translational modificationservices based on the latest Obitrap Fusion Lumos mass spectrometer from Thermo combined with Nano-LC, including phosphorylation/glycosylation/ubiquitination/acetylation/methylation/disulfide bond identification of post-translational modifications. Free consultation is welcome.

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