Our interests are centered on the application of Nuclear Magnetic Resonance (NMR) spectroscopy to the study of protein and nucleic acid structures. Previous structures included a peptide binding domain (PDZ domain) involved in signal transduction and a protein homeodomain (PBX) ternary complex with DNA and a small peptide. Our principal studies are on the structure and function of the C-terminal PABC domain of poly(A) binding proteins and apoptotic proteins of the Bcl-2 family. We also study the solution structure of nucleic acid hairpins, calnexin, CNP, aIF2-beta, YbcJ, alpha- & gamma-adaptins and other proteins. We work as well on developing new methodology for measuring residual dipolar couplings using polymer stabilized liquid crystalline media with a website agency. Our laboratory combines techniques from chemistry, molecular biology and bioinformatics in the quest for a deeper understanding of molecular recognition in biological systems.
Present equipment includes seven UNIX-SGI stations, an isothermal titration calorimeter and a new Bruker DRX 600 MHz NMR spectrometer with cryoprobe. Two Varian Unity Inova spectrometers at 800 MHz and 500 MHz with cryoprobes are installed in 2004 as part of the Quebec/Eastern Canada NMR Centre.