Elucidating the structure-function relationships of membrane proteins is critical for the design of therapeutic agents to treat disease and for understanding numerous cellular processes such as signal transduction and molecular or ion transport. Recent advances in the application of correlated single molecule imaging techniques have provided new insights into protein-protein and protein-membrane interactions. To demonstrate the potential of these approaches, we have used in situ atomic force microscopy and single molecule fluorescence microscopy to characterize the interactions between membrane receptors and their soluble ligands, examine the monomer-dimer equilibrium in a family of adhesion receptors, and elucidate protein-mediated membrane restructuring of a supported lipid bilayer. Building on these studies, we examined the CorA ion transporter protein. We demonstrated single molecule resolution of reconstituted CorA molecules in supported lipid bilayers using a correlated AFM-TIRF microscopy platform. This approach provided new insights into a purported mechanism of CorA activation that involved ion binding.
| Identifer | oai:union.ndltd.org:TORONTO/oai:tspace.library.utoronto.ca:1807/18287 |
| Date | 15 January 2010 |
| Creators | El Masri, Ghaleb |
| Contributors | Yip, Christopher M. |
| Source Sets | University of Toronto |
| Language | en_ca |
| Detected Language | English |
| Type | Thesis |
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