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Team:Queens Canada/ChimeriQ
From 2012.igem.org
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| + | This year, our team is investigating new methods of increasing the efficiency of bioremediation and biosynthesis using modified bacteria. The development of the oil sands in Alberta, has resulted in the build up of toxic byproducts stored in massive tailings ponds. To help resolve these issues, our goals can be divided up into three main categories: the binding of pollutants, adhesion and aggregation of bacteria, and catalysis. | ||
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| + | Most bacteria possess tail-like appendages called flagella, which can be genetically altered for novel functions. Each flagella is made up of a number of polymerizing proteins, often called flagellin. By making chimeric insertions in the variable domain of the flagellin, we can incorporate metal binding proteins, enzymes, adhesive proteins as well as scaffolding proteins to further extend the possible applications. To accomplish this, we can summarize the majority of our work into three main tasks: | ||
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| + | clone and modify the constant domains of the flagellin protein for making insertions using Biobricks and parts obtained from the wild. | ||
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| + | design a flexible, compatible cloning method for efficientlymaking chimeric insertions using Biobricks and other parts | ||
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| + | introduce binding and catalysis to the length of the flagella. | ||
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Revision as of 23:59, 3 October 2012
Control
ChimeriQ - Description
Overview
This year, our team is investigating new methods of increasing the efficiency of bioremediation and biosynthesis using modified bacteria. The development of the oil sands in Alberta, has resulted in the build up of toxic byproducts stored in massive tailings ponds. To help resolve these issues, our goals can be divided up into three main categories: the binding of pollutants, adhesion and aggregation of bacteria, and catalysis.
Most bacteria possess tail-like appendages called flagella, which can be genetically altered for novel functions. Each flagella is made up of a number of polymerizing proteins, often called flagellin. By making chimeric insertions in the variable domain of the flagellin, we can incorporate metal binding proteins, enzymes, adhesive proteins as well as scaffolding proteins to further extend the possible applications. To accomplish this, we can summarize the majority of our work into three main tasks:- clone and modify the constant domains of the flagellin protein for making insertions using Biobricks and parts obtained from the wild.
- design a flexible, compatible cloning method for efficientlymaking chimeric insertions using Biobricks and other parts
- introduce binding and catalysis to the length of the flagella.
Fluorescence
Catalysis
CohDoc
