CANADA
Jean-Francois Couture
Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Canada
INPEC node since 2014
The Couture laboratory is focused on fundamental questions regarding the interactions between proteins and chromatin. This includes understanding how post-translational modifications of chromatin influence chromosome structure, as well as investigating how mutations associated with cancers like leukemia disrupt epigenetic processes. Ultimately, the laboratory uses the insights gained from these studies to engineer small molecules, aiming to develop novel modalities for treating diseases.
Keywords: epigenetics, chromatin, nucleosome, X-ray crystallography, histone modifying enzymes
Martin Schmeing
Department of Biochemistry, McGill University, Montreal, Canada
INPEC node since 2010
The general goal of the lab is to understand how some of the large enzymes in the cell act to perform their important functions. To do this, we combine X-ray crystallography, electron microscopy, biochemical techniques and chemical biology. The main current focus of the lab is the study of nonribosomal peptide synthetases (NRPSs), large macromolecular machines that, like the ribosome, catalyze peptide bond formation. Instead of making proteins, these enzymes produce a large variety of small molecules with important and diverse biological activity. For example, NRPSs synthesize anti-fungals, anti-bacterials, anti-virals, anti-tumourigenics, siderophores, and immunosuppressants, including classic therapeutics such as penicillin and cyclosporin, and modern billion-dollar antibiotics like daptomycin.
Keywords: megaenzyme, NRPS, natural products, X-ray crystallography, electron microscopy, ribosome
Sophie Gobeil
Department of Biochemistry, Microbiology and Bioinformatics,
Université Laval, Quebec City, Canada
INPEC node since 2026
The Gobeil laboratory investigates how protein structure and conformational dynamics drives immune evasion, antigen-antibody recognition, and host-pathogen interactions. We study viral fusion proteins, antibodies, and host receptors to understand how mutations and glycosylation impact molecular recognition, epitope exposure, and viral entry. Our integrative structural biology approach combines X-ray crystallography, cryo-electron microscopy (cryo-EM), and nuclear magnetic resonance (NMR) with biochemical, biophysical, and computational analyses, including molecular dynamics simulations. By linking protein structure and dynamics to function, we aim to inform protein engineering and immunogen design efforts for the development of therapeutics for infectious diseases.
Keywords: viral fusion proteins, antibody, glycans, X-ray crystallography, electron microscopy, host-pathogen interactions
