800 MHz NMR
Proteins are large, essential biological molecules that regulate and participate in all cellular processes. Some proteins are enzymes that catalyze biochemical reactions, while others maintain cell shape, participate in cell signaling, immune responses, cell adhesion, and the cell cycle. Their roles in human health and disease (such as cancer, cystic fibrosis, neurodegenerative diseases) is the subject of intense research worldwide.
Simon Sharpe and Dave Davidson gather solid state NMR data
An understanding of the role played by a protein in cellular function requires a detailed picture of its three-dimensional structure and its interactions with other proteins, as well as an appreciation of how the structure varies as a function of time due to molecular dynamics. Over the past decade multi-dimensional, multi-nuclear solution nuclear magnetic resonance (NMR) spectroscopy has become a powerful technology for obtaining both structural and dynamical information on macromolecules and their complexes, including disordered proteins.
The importance of NMR is underscored by the fact that it is the only technique that can provide atomic level resolution information about biomolecular structure and dynamics in the solution state, that approximates the natural milieu of these molecules.
In the NMR experiment the unique magnetic environment of NMR active probes (for example 1H, 15N, 13C nuclei) is studied, and this environment reports directly on the structure and interactions of the biological molecule. Because the experiments are often carried out in solution, it is possible to obtain information easily under a variety of different conditions, including varying amounts of an interacting partner, on well-folded or highly mobile protein regions.
The resulting data can provide significant insights into function, regulation and binding of proteins and protein complexes, including those that are potential or actual targets for therapeutic interventions.
Equipment and Resources
The NMR Center at the University of Toronto houses a variety of state of the art NMR spectrometers for studies of biomolecular structure and function. These include instruments operating at 500 MHz, 600 MHz, 700 MHz, 800 MHz and 1GHz (to be installed summer 2019). Notably, the 1GHz NMR spectrometer will be only the second such instrument to be in operation and the first to employ active shielding that sequesters the magnetic footprint of the machine so that it can be installed in a relatively small area.
Instrumentation is available both for studies in the solution and solid state, over a wide range of different sample conditions.
Upkeep is provided by a PhD level NMR manager with multiple decades of experience that ensures a smooth operation of equipment with minimal downtime.
Location
Medical Sciences Building, 1st Floor
Contacts
Lewis E. Kay
Medical Sciences Building, Room 1233
1 King's College Circle
416-978-0741
kay@pound.med.utoronto.ca
Simon Sharpe
Peter Gilgan Center for Research and Learning
686 Bay St., Room 20.9714
416-813-7852
ssharpe@sickkids.ca