Proteomics /Mass spectrometry

Research interest

Determination of phosphorylation PTM sites in proteins
Post translational modification (PTM) of proteins plays a key role in the control of a wide range of biological functions and activities. Thus, development of technologies for the rapid and conclusive identification of PTMs is essential. Such modified proteins are often present in sub-stoichiometric amounts compared to the unmodified protein, and the chemical nature of the modification can hinder mass spectrometry analysis. By enriching the sample for the specifically modified form of the protein/peptide, the chances of identifying the modified peptide during mass spectrometric analysis are greatly improved. We plan to assemble a two-dimensional nano-flow liquid chromatograpy system where the first dimension is phosphorylated peptide enrichment, the second is separation of these eluted peptides, with subsequent mass spectrometric identification of phosphorylated sites.

Services

mass spectrometric analysis of in-gel and in-solution protein(s).