Supporting data for "EXPLORATION OF 3-NITROTYROSINE AND 3-AMINOTYROSINE-CONTAINING PROTEINS WITH A SYNTHETIC PROBE"

In our study, we focus on developing a new method to identify some proteins with tyrosine modifications using synthetic probes. Tyrosine, a vital amino acid that comprises approximately 3.2% of protein composition, is subject to a range of post-translational modifications (PTMs), including nitration, phosphorylation, hydroxylation, halogenation, and sulfation. These PTMs play crucial roles in regulating protein functions, cellular signalling, homeostasis, and a host of biological processes. A well-studied PTM, protein tyrosine nitration (PTN), arises from oxidative and nitrative stress. Therefore, we developed a selective detection method using a synthetic probe to identify proteins with tyrosine modification. Utilizing the probe, we successfully labelled and enriched numerous proteins with tyrosine modifications in RAW264.7 cells.
Afterwards, we selected two targets for further investigation into the effects of tyrosine modifications on their functions. By using the purifying site-specific modified proteins, it revealed that tyrosine modification indeed affected protein function at different sites.