Protein-protein interactions and post-translational modifications (PTMs) are the major events which regulate signaling cascades in the cells. In disease states, these modification networks get altered disrupting normal cellular processes. Understanding the modifications of a particular cell or protein network in diseased and normal states will provide insight into the physiological and pathological processes of those diseases at a molecular level. The major challenge at this moment is the reliable identification and quantification of protein networks and post-translational lipid modifications in large-scale studies. PTM abundances are low, and their different structures require the development of new methods to suitably identify them with confidence in large-scales samples. A mass spectrometer is indispensable in proteomics research due to its sensitivity and speed. Chemistry-based approaches combined with mass spectrometry have become very popular due to their ability to enrich low abundance modifications; furthermore, different features can be implemented in the chemical probes so they can be confidently identified by mass spectrometry. In this regard, mass spectrometry cleavable strategies are also very popular because the modified peptides can be tracked by the signature mass generated in the mass spectra. This signature mass allows large-scale samples to be analyzed very efficiently. In this seminar, several chemical proteomics methods will be presented, which can be utilized for identifying large-scale protein-protein interaction networks and lipid modifications of proteins.


Saiful Chowdhury (University of Texas, Arlington)