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Our initial approach was to include two identical cellulose-binding domains on either side of the streptavidin domain. However, this led to numerous problems with molecular cloning due to the repetitive nature of the sequence. We changed our approach to using two cellulose-binding domains with different sequences. This allowed us to successfully conduct the molecular cloning.
The goal of this subproject is to create a cellulose cross-linking protein to increase material strength and allow for the modular attachment of biological sensors. This fusion protein contains two distinct cellulose-binding domains on either side of a streptavidin domain. The cellulose-binding domains cross link the cellulose fibers while the streptavidin serves as a binding domain for biological sensors. Streptavidin has a strong affinity for biotin thus, a cell expressing an outer membrane protein that has been biotinylated will bind tightly to this domain. This will allow our UAV to make use of a number of biological sensors.
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Results
Our initial approach was to include two identical cellulose-binding domains on either side of the streptavidin domain. However, this led to numerous problems with molecular cloning due to the repetitive nature of the sequence. We changed our approach to using two cellulose-binding domains with different sequences. This allowed us to successfully conduct the molecular cloning.
Methods & Safety
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