Protein Structure and Dynamics
Our research involves both analytical and computational modeling. Our computation projects focus on: Intrinsically disordered proteins, atomic simulations of solvent-mediated interactions, biophysical models of protein evolution, cooperativity and nonnative interactions in folding, mathematical basis of type-2 topoisomerase action. For the computational effort, we employ codes developed by ourselves for coarse-grained biomolecular modeling as well as common molecular dynamics packages.
The Davidson laboratory focuses on bacteriophages, the viruses that infect bacteria. They investigate how phages work, and how phage-derived entities can be utilized for applications in human health. We also have discovered and study anti-CRISPRs, which are phage-encoded inhibitors of CRISPR-Cas systems. We endeavour to understand how they work, and how they can be exploited in genome editing applications.
Ernst Lab
Our research focuses on transmembrane signaling by G protein-coupled receptors (GPCRs). We seek to elucidate GPCR functionality and interaction with signaling proteins like G proteins and arrestins. Using different spectroscopic techniques and X-ray crystallography, we investigate the mechanisms, specificity, and structural basis of these interactions. Another focus of our work is on rhodopsin, the photoreceptor protein in the vertebrate retina.
The Forman-Kay lab works on projects relevant to cancer and neurobiology. They investigate the phase separation of disordered proteins in RNA processing bodies, a key regulatory process for neurological function. Their work also offers widely recognized contributions to the fields of intrinsically disordered proteins, protein interaction domains, and cystic fibrosis transmembrane conductance regulator (CFTR) structure, dynamics, and interactions.
Our research activities are focused on understanding at the molecular and cellular level biological processes involved in microbial pathogenesis. The insights we gain from our fundamental research are used to develop novel strategies and treatments for bacterial and fungal biofilm related infections.
In the Julien lab, we seek a molecular understanding of glycoproteins associated with immune function to provide roadmaps for the design of improved vaccines, and immunotherapies against cancers and autoimmune diseases. Dr. Julien’s laboratory characterizes surface glycoprotein receptors by using a combination of biochemical, biophysical, immunological and structural techniques.
Our research focuses on the development and function of blood platelets. These tiny cells co-ordinate blood clotting at wound sites by adhering, aggregating, and secreting a wide variety of molecules. Platelets are also involved in the formation of arterial plaques and pathological clots. Our particular interest is alpha granules, vesicles that platelets use to transport and secrete specialized proteins.
Research in the Kay laboratory spans a range of disciplines from spectroscopy and biophysics through to biochemistry. Two major areas of interest include: NMR of Supra-Molecular Machines, and Characterizing Low populated states of proteins.
Keeley Lab
The Keeley Lab researches the structure, mechanisms of self-assembly, and evolutionary history of elastins and elastomeric proteins. We focus on the regulation of protein expression in development and disease, and consider the effects of sequence variations on the elastomeric properties of the resultant polymers. We use a structural approach alongside computational chemistry, solid state and solution NMR, and bioinformatics.
The Maxwell lab focuses on interactions of bacteria with bacteriophages - viruses that infect bacteria. We leverage a multi-disciplinary approach, combining expertise in phage biology, structural biology, and bioinformatics, with detailed in vitro and in vivo studies to investigate new areas in phage biology. Current projects focus on anti-phage defence and characterizing the dark matter of phage genomes.
Melnyk Lab
Using chemical biology and targeted drug discovery approaches combined with molecular biophysics and structural analysis the Melnyk Lab seeks to understand bacterial toxins associated with infectious disease. We identify and validate host & toxin targets and discover small molecule hits for further exploration and development.
Our lab focuses on the structural and functional characterization of protein and ion translocation machineries within the membranes of pathogenic bacteria. We use primarily X-ray crystallography in combination with other molecular approaches to gain a detailed understanding of how these membrane protein complexes function.
Norris Lab
Research in the Norris lab investigates the structure and molecular assembly of deadly RNA viruses, with a special emphasis on paramyxoviruses (measles virus, mumps virus, Nipah virus, parainfluenza virus) and filoviruses (Ebola virus & Marburg virus). We use structural biology (X-ray crystallography and electron cryomicroscopy), functional biochemistry, cellular biology, and basic virology to understand the molecular mechanisms driving viral self-assembly.
Ohh Lab
Our research mission is to elucidate the molecular mechanisms governing the function of two major cancer-associated proteins called von Hippel-Lindau (VHL) tumour suppressor protein and RAS oncoprotein with the supposition that lessons learned would provide fundamental understanding of cell biology and lay the basic foundation for the development of rational anti-cancer therapeutics.
The Pomès group specializes in the development of computational methods and their application to the study of biological processes. In particular, we seek to uncover the link between the structure, dynamics, and function of proteins. Our work is grounded in statistical mechanics, which provides a formal connection between microscopic and macroscopic length scales.
Privé Lab
Our research centers on the study of protein structure and molecular recognition, with an emphasis on understanding protein-protein, protein-peptide and protein-lipid interactions.
Dr. Gil Privé
Our research focuses on dynamics and mechanisms of complex biological processes such as: Protein folding, PrP and amyloidosis, Enzyme functional dynamics, GPCR functional dynamics, Direct molecular imaging of proteins and nanoparticles by MRI
Rini Lab
Our group, consisting of biophysicists and biochemists, studies the structure and function of macromolecular assemblies using electron cryomicroscopy (cryo-EM), image analysis, biochemistry and molecular genetics.
Our group, consisting of biophysicists and biochemists, studies the structure and function of macromolecular assemblies using electron cryomicroscopy (cryo-EM), image analysis, biochemistry and molecular genetics.
Research in the Sharpe lab focuses on mechanisms of peptide/protein self-assembly, and the links between sequence, structure, and activity of the resulting macromolecular assemblies. We use a wide range of biophysical tools, which an emphasis on applying solid state and solution NMR spectroscopy to achieve a molecular-level understanding of protein structure and dynamics.
Research in the Sicheri Lab is focused on elucidating the mechanism of action of signalling molecules through the use of X-ray crystallography and biochemical techniques.
In the Watts lab we use a multifaceted approach to study the pathogenesis of the prion and related diseases that involves recombinant proteins, cultured cells, and transgenic mice. Our research utilizes techniques from the fields of biochemistry, biophysics, neuropathology, and cell biology to better understand diseases such as Alzheimers, Parkinson’s and Creutzfeldt-Jakob Disease.
Yip Lab
Research at the Yip Lab focuses on the development and application of super-resolution combinatorial microscopies for imaging of molecular assemblies, structures, and dynamics. Recent projects include studies of peptide and protein-membrane interactions in the context of neurodegenerative diseases, the design of novel antimicrobial agents, and membrane receptor self-association with implications for cell signaling in infection and cancers.