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− | <h4 align="center">Out of the 16 parts we submitted, our best characterized part was<a href="http://parts.igem.org/Part:BBa_K2083010"> BBa_K2083010</a>. BBa_K2083010 was one of the uniquely mutated eGFP reporter proteins. In addition to a 5' untranslated region, designed to be the target binding site of the dCas9 protein, we designed the protein to have a mutated start codon. The normal start codon, that was included in the "wild type", was ATG. Our mutant had an ACG start codon. The ACG eGFP mutant was tested using fluorescence microscopy and was further confirmed using flow cytometry as part of a <a href="https://2016.igem.org/Team:WPI_Worcester/Collaborations">collaboration</a> with the Boston University Wetlab team. Both of these techniques showed that the ACG GFP mutant had a significantly lower level of fluorescence, indicating a significantly decreased level of expression of the mutant gene</h4> | + | <h4 align="center">Out of the 16 parts we submitted, our best characterized part was<a href="http://parts.igem.org/Part:BBa_K2083010"> BBa_K2083010</a>. BBa_K2083010 was one of the uniquely mutated eGFP reporter proteins. In addition to a 5' untranslated region, designed to be the target binding site of the dCas9 protein, we designed the protein to have a mutated start codon. The normal start codon, that was included in the "wild type", was ATG. Our mutant had an ACG start codon. The ACG eGFP mutant was tested using fluorescence microscopy and was further confirmed using flow cytometry as part of a <a href="https://2016.igem.org/Team:WPI_Worcester/Collaborations">collaboration</a> with the Boston University Wetlab team. Both of these techniques showed that the ACG GFP mutant had a significantly lower level of fluorescence, indicating a significantly decreased level of expression of the mutant gene.</h4> |
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Latest revision as of 20:45, 19 October 2016