The Laboratory is broadly interested in the development and application of proteomic techniques that facilitate understanding of biological systems at the molecular level. There is a particular emphasis on several lines of research:

  1. Biochemical approaches to enrich and characterize post-translationally modified peptides and proteins. A key aspect of large-scale PTM characterization is the ability to enrich specific classes of modified peptides. Examples include: TiO2 chromatography for the enrichment of phosphopeptides; immobilized lectin chromatography for the enrichment of glycopeptides; anti-acetyllysine antibodies for the enrichment of acetylated peptides; anti-GlyGly remanant antibodies for the enrichment of peptides bearing a ubiquitin attachment sites; biotin-capture and release approaches for enriching persulfidated peptides.
  2. The development and application of large scale techniques that enable quantitative comparisons between cells or tissue in distinct physiological states. We have extensive experience with label-free quantification using the intensity of the top three peptides on a Synapt G2S equipped with ion mobility. We also commonly use stable isotope labeling strategies such as iTRAQ or TMT.
  3. Proteomic applications of Ion Mobility Spectrometry, particularly with respect to the previous two research aims.
While these techniques can be applied across all areas of biology, we are particularly interested in using mass spectrometry to aid in the study of the central nervous system. We have extensively characterized connections between neurons known as synapses. This work allows us to identify and quantitatively profile over 1,000 proteins in post-synaptic spine heads (the structures in neurons responsible for receiving and processing signals from neurons upstream in a synaptic signaling network). Post-translational modifications (such as phosphorylation, O-GlcNAcylation, ubiquitination, and acetylation) on proteins alter their behavior in a number of ways, including affecting enzyme kinetics, protein turnover, protein-protein interactions and protein sub-cellular localization. We are interested in using mass spectrometry to characterize molecules in the nervous system and use this data to gain a deeper understanding into synaptic physiology.