|Dr. Mazdak Khajehpour
The Khajehpour group studies interactions that cause proteins to fold correctly. Folding processes in proteins are studied both from kinetic and thermodynamic standpoint. The techniques used in these studies are steady-state and time-resolved fluorescence spectroscopy, differential scanning calorimetry, stopped-flow and temperature-jump relaxation spectroscopy.
|Dr. Sean McKenna
We study the structural and molecular biology of protein-nucleic acid interactions. We are focused on understanding (i) the role of RNA-protein interactions in mediating the host cell immune response to viral infection, and (ii) investigating RNA quadruplex structures and their interactions with quadruplex-specific helicases.
|Dr. Joe O'Neil
Proteins carry out their biological functions through changes in conformation. We measure protein dynamics by NMR spectroscopy and hydrogen exchange chemistry to determine the timescale and magnitude of the conformational changes that explain the activities of a membrane protein, an HIV transcription activator and a viral enzyme.
|Dr. Hélène Perreault
Our laboratory uses mass spectrometry, especially matrix-assisted laser desorption/ionization (MALDI), to study the composition and structure of proteins, glycoproteins and oligosaccharides. Glycans found in antibodies are a main focus area and for these we develop sample preparation techniques using pull down, chromatography and electrophoresis to make samples amenable to mass spectrometry. We also use electrospray ionization (ESI-MS).
|Dr. John Sorensen
The Sorensen group has an ongoing research program that is focused on the biosynthesis of natural products. Our main interest is the biosynthesis of polyketide natural products in lichen and other fungi. We are also examining the biosynthesis of novel natural products in soil fungi. We have other projects aimed at the synthesis of small molecules with biological applications.
|Dr. Jörg Stetefeld
The primary goal of our research is to understand in detail the structure-function relationship of proteins as dynamic systems. We are mainly focused on signaling linked to catalytic turnover, the storage function of coiled-coil domains and mechanisms of complex formations and signal transduction within the extracellular matrix.