John E Baenziger

Carte électronique

John E Baenziger
Full Professor

B.Sc. (Hons), Queen's University (1984)
Ph.D., University of Ottawa (1989)
Post-Doctoral Fellow, Harvard Medical School and Boston University (1989-1992)
Premier's Research Excellence Award
John Charles Polanyi Prize for Doctoral Research

Pièce : Room 4216, Guindon Hall
Bureau : 613-562-5800 poste 8222
Courriel professionnel :

John Baenziger


Research Interests:

There are two main research projects in my laboratory funded by grants from the Canadian Institutes of Health Research (CIHR) and the Natural Sciences and Engineering Research Council of Canada (NSERC). Both involve the structural characterization of integral membrane proteins using biophysical methods.

The first is titled "Structure and function of the nicotinic acetylcholine receptor in its membrane environment". The nicotinic acetylcholine receptor (nAChR) is a neurotransmitter-gated ion channel found at synapses located in both the nervous system and at neuromuscular junctions. The nAChR (and other homologs) plays a central role in rapid communication in the brain. Factors that influence the efficacy of synaptic communication play an important role in higher brain functions, such as memory and learning, etc. Lipids are potent modulators of nAChR function. Increasing evidence suggests that lipids play an important role modulating nAChR function under both normal and pathological conditions. The goal of this research project is to understand the mechanisms by which lipids influence nAChR function in order to ultimately understand the role of lipid-nAChR interactions in brain function in general.

The second project is titled "Structural characterization of proteins involved in iron uptake in Campylobacter jejuni". C. jejuni is a common food borne pathogen that leads to food poisoning and in severe cases death. Like all gram negative bacteria, C. jejuni has an obligate requirement for exogenous iron and thus exhibits a complex mechanism for "stealing" iron from the human intestine. One membrane protein, called CfrA, is central to iron uptake and is a potential drug-target. We seek to understand the mechanisms by which CfrA transports iron across the outer membrane in order to develop mechanisms for inhibiting function. We are solving the crystal structure of CfrA. Using the defined crystal structure and a homology model as a guide, modern molecular biological tools are now being used to define the mechanisms of iron transport.

The laboratory is well equipped with basic biochemical equipment including Acta FPLC, cell culture incubators, a Nikon SMZ800 microscope, and a DynaPro dynamic light scatterer. There are three modern FTIR spectrometers, including a new FTS 7000 from Varian. These are equipped with numerous FTIR data acquisition accessories, including standard ATR sampling accessories, a Golden Gate diamond ATR, and both manual and automated polarizers. The FTIR systems have been fully automated for measuring difference and absorbance spectra as a function of both light polarization and temperature. The lab is also equipped with a Cary Eclipse fluoresence spectrometer. We have access to electrophysiological equipment.


neurotransmitter receptors, Cys-loop receptors, nicotinic acetylcholine receptors, synaptic efficiency, allosteric modulation, protein structure function, lipid-protein interactions, spectroscopy, electrophysiology, crystallography

Champs d'intérêt

  • The role of nicotinic acetylcholine receptors in health and disease
Haut de page