Our interests are centered on the application of Nuclear Magnetic Resonance (NMR) spectroscopy to the study of protein and nucleic acid structures. Earlier 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. We also studied the solution structure of nucleic acid hairpins, and CNP, RICH, GlgS, YbeD, aIF2-beta, CsrA, YbcJ, TcUBP1, GatB, YggX, ChaB, NECAP1, alpha- & gamma-adaptins and other proteins. Our principal studies are on the structure and function of the poly(A) binding proteins (PABC, RRM, etc.), the ER interactome (calnexin, ERp57, PDI, etc.) and apoptotic proteins of the Bcl-2 family (Bcl-w, Bcl-xL, Bak, Mcl-1, tBid, etc.). We work as well on developing new methodology for measuring residual dipolar couplings using polymer stabilized liquid crystalline media. 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 ten UNIX-SGI and Linux-PC stations, an isothermal titration calorimeter and Bruker DRX 600 MHz NMR spectrometer with cryoprobe. Two Varian Unity Inova spectrometers at 800 MHz and 500 MHz are installed as part of the Quebec/Eastern Canada NMR Centre.

BCL-w, Denisov et al. (2003), J.Biol.Chem. 278(23):21124-21128

"Facilitating the development of anticancer drugs"
About us in McGill University Media Releases

BAK dimer, Moldoveanu et al. (2006), Mol. Cell, 24(5):677-688