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Team:StanfordBrownSpelman/Cellulose Cross Linker
From 2014.igem.org
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| - | 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. The interaction between SA (streptavidin) and biotin is one of the strongest non-covalent interactions in nature [ | + | 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[1] 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. The interaction between SA (streptavidin) and biotin is one of the strongest non-covalent interactions in nature [2]. Therefore 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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<h5><center>References</h5> | <h5><center>References</h5> | ||
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| - | + | 1. M Linder and T T Teeri (1996) The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose. <i>PNAS.</i> 55. PMID: <a href="http://www.ncbi.nlm.nih.gov/pmc/articles/PMC37976/</a>.<br> | |
| + | 2. Chivers, Claire <i>et al.</i> (2011) How the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer. <i>Biochem. J.</i> 12251. PMID: <a href="http://www.ncbi.nlm.nih.gov/pubmed/21241253">24136966</a>.<br> | ||
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Revision as of 19:06, 16 October 2014
Cellulose Cross-Linker
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[1] 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. The interaction between SA (streptavidin) and biotin is one of the strongest non-covalent interactions in nature [2]. Therefore 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.
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[1] 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. The interaction between SA (streptavidin) and biotin is one of the strongest non-covalent interactions in nature [2]. Therefore 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.
Methods
Methods here.
