My laboratory focuses on the protein chemistry of GABAA receptors to identify and characterize drug binding sites, sequence variants and post-translational modifications as well as to define the protein complexes in which GABAA receptors reside in vivo. A variety of biochemical and molecular biological approaches are applied to these problems, with particular emphasis on high-resolution mass spectrometry.

The lab has a longstanding interest in identifying the sites to which anesthetics bind to produce their effects. We have focused on anesthetic neurosteroids, using neurosteroid analogue photolabeling reagents to covalently label protein binding sites and identifying the sites of incorporation using protein mass spectrometry.

The lab has also pioneered methods for mass spectrometric methods to sequence the transmembrane segments of native GABAA receptor from picomole quantities of protein. Current directions in the lab include: 1) Studies of dynamic regulation of protein phosphorylation (particularly ion channels) in native brain using global (“shotgun”) mass spectrometric techniques and 2) Identification of GABAA-receptor associated proteins in brain using immunopurification coupled to mass spectrometry with label-free quantitation.