Team:StanfordBrownSpelman/Cellulose Cross Linker

From 2014.igem.org

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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> 
                         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> 
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  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 19:07, 16 October 2014

Stanford–Brown–Spelman iGEM 2014 — Cellulose Acetate

Methods
Methods here.


Figure 1. Figure caption here.
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.
References
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. PNAS. 55. PMID:
Additional Information
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