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
  2. The development and application of large scale techniques that enable quantitative comparisons between cells or tissue in distinct physiological states
  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.