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Team:Illinois/Bimolecular Fluorescence
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| - | We hope to design a soluble molecular biosensor that, when it comes in contact with an 'activating' ligand such as a virus, bacterium, or specific antibody, generates a fluorescent response using bimolecular complementation. Traditionally unimolecular constructs such as Green Fluorescent Protein (GFP) can be split into two heterologous protein fragments, which can then bind and reinitiate fluorescence upon close spatial proximity. GFP fragments are often fused to endogenous intracellular proteins to study protein-protein interactions: complementation between these GFP fragments is achieved only when they are tethered to proteins which interact strongly. | + | We hope to design a soluble molecular biosensor that, when it comes in contact with an 'activating' ligand such as a virus, bacterium, or specific antibody, generates a fluorescent response using bimolecular complementation. Traditionally unimolecular constructs such as Green Fluorescent Protein (GFP) can be split into two heterologous protein fragments, which can then bind and reinitiate fluorescence upon close spatial proximity. GFP fragments are often fused to endogenous intracellular proteins to study protein-protein interactions: complementation between these GFP fragments is achieved only when they are tethered to proteins which interact (bind) strongly. |
| - | We seek to harness this powerful molecular tool for an inverse task: instead of studying putative interactions between known proteins, we are designing fusion constructs to detect the presence of proteins known a priori to interact. | + | We seek to harness this powerful molecular tool for an inverse task: instead of studying putative interactions between known proteins, we are designing fusion constructs to detect the presence of proteins known ''a priori'' to interact, as a one-step diagnostic assay. For example, |
Revision as of 02:44, 12 June 2008
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Bimolecular Fluorescence Biosensor
Core Team Members
Luke Edelman, Adam Zoellner, Meghan McCleary, Katrina Keller
Project Summary
We hope to design a soluble molecular biosensor that, when it comes in contact with an 'activating' ligand such as a virus, bacterium, or specific antibody, generates a fluorescent response using bimolecular complementation. Traditionally unimolecular constructs such as Green Fluorescent Protein (GFP) can be split into two heterologous protein fragments, which can then bind and reinitiate fluorescence upon close spatial proximity. GFP fragments are often fused to endogenous intracellular proteins to study protein-protein interactions: complementation between these GFP fragments is achieved only when they are tethered to proteins which interact (bind) strongly.
We seek to harness this powerful molecular tool for an inverse task: instead of studying putative interactions between known proteins, we are designing fusion constructs to detect the presence of proteins known a priori to interact, as a one-step diagnostic assay. For example,
