The research aims of the Columbus laboratory are two fold:

  1. to address the challenges in membrane protein structural biology, and
  2. to investigate the structural determinants of bacterial pathogen – host interactions mediated by membrane proteins. Specifically, the structures of neisserial Opa proteins are of interest.

A major obstacle to membrane protein structure determination is the selection of a detergent micelle or lipid vesicle that mimics the native lipid bilayer. Currently, membrane mimetics are selected by exhaustive screening because the effects of protein-amphiphile interactions on protein structure are so poorly understood. The overall goal is to use a multifaceted approach (NMR and EPR spectroscopy, small angle X-ray scattering, and X-ray crystallography) to develop a fundamental understanding of the protein-amphiphile interaction, accelerating structural determination and functional characterization of membrane proteins involved in bacterial pathogenesis