Irina Perdivara, Ph.D.
Post translational modifications of proteins represent key biological events affecting their cellular localization, physiological conformation and functions. For a complete understanding of structure-function relationship of proteins, site specific characterization of PTMs is required, but this process is not always straightforward. In particular, glycosylation is one such challenging modification, because the biological heterogeneity and physico-chemical properties of glycans/glycopeptides render their analysis difficult for most of the techniques available at the present. My research efforts are aimed at identification of N- and O-glycosylated structures in proteins associated with various diseases by mass spectrometry. The analytical approach I typically employ combines proteolytic degradation of proteins, liquid chromatographic separation, and analysis of glycopeptides by collision induced dissociation and electron transfer dissociation. Several of my ongoing projects include: determination of O-linked glycosylation and O-GlcNAcylation in amyloid precursor protein(s), characterization of O-glycosylation sites and cross-linking analysis of collagens, characterization of age-dependent glycosylation changes in cartilage. One further research interest is peptide mapping and de novo sequence determination of proteins for which no genomic information is available (e.g. antibodies produced by hybridoma technology). In addition to elucidation of primary structure, my efforts are focused at the understanding of fragmentation pathways of protonated peptides undergoing rearrangements during collision induced dissociation.
Irina Perdivara, Ph.D., is a research fellow in the Mass Spectrometry Group within the Laboratory of Structural Biology. She received her Diploma and Ph.D. degrees from the University of Konstanz, Germany.