Progress of Analytical Methods for Protein Cysteine Post-translational Modifications
Abstract Cysteine thiols have high reaction activity as sites of nucleophilic, redox catalysis, metal binding and allosteric regulation, and play significant roles in protein structures and functions. Due to the reactivity of the thiol group, cysteine residues are very prone to post-translational modifications (PTMs) such as oxidation, lipidation, and so on, which can regulate/damage protein functions, and are associated with many diseases. Thus, it is very important to qualitatively and quantitatively analyze PTMs in the cysteine residues for further understanding its biological functions. This review mainly focuses on the development of mass spectrometric and high-throughput proteomic approaches for investigating some common cysteine post-translational modifications.