http://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&feed=atom&action=historyTeam:Arizona State/Data - Revision history2024-03-28T10:52:06ZRevision history for this page on the wikiMediaWiki 1.16.0http://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=281654&oldid=prevEqin at 05:53, 26 October 20122012-10-26T05:53:02Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h2>Current Research</h2></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h2>Current Research</h2></div></td></tr>
</table>Eqinhttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=277402&oldid=prevEthan ward at 04:03, 25 October 20122012-10-25T04:03:44Z<p></p>
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</table>Ethan wardhttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=276902&oldid=prevAbhinavmarkus at 23:42, 24 October 20122012-10-24T23:42:09Z<p></p>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=274348&oldid=prevMhsands at 06:03, 23 October 20122012-10-23T06:03:02Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h2>Topoisomerase-based DNA Biosensor</h2></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h2>Topoisomerase-based DNA Biosensor</h2></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Current testing with the split beta-galactosidase system includes time-interval testing of colorimetric response, including quantitative measurements of beta-galactosidase concentration over time, omega fragment negative control testing, and in vitro testing of the alpha and omega fragments linked to streptavadin and Magainin.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Current testing with the split beta-galactosidase system includes time-interval testing of colorimetric response, including quantitative measurements of beta-galactosidase concentration over time, omega fragment negative control testing, and in vitro testing of the alpha and omega fragments linked to streptavadin and Magainin.</div></td></tr>
</table>Mhsandshttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272926&oldid=prevAbhinavmarkus at 19:03, 21 October 20122012-10-21T19:03:01Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272925&oldid=prevAbhinavmarkus at 19:02, 21 October 20122012-10-21T19:02:37Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272923&oldid=prevAbhinavmarkus at 19:02, 21 October 20122012-10-21T19:02:12Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272922&oldid=prevAbhinavmarkus at 19:02, 21 October 20122012-10-21T19:02:01Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272920&oldid=prevAbhinavmarkus at 19:01, 21 October 20122012-10-21T19:01:15Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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</table>Abhinavmarkushttp://2012.igem.org/wiki/index.php?title=Team:Arizona_State/Data&diff=272919&oldid=prevAbhinavmarkus at 19:00, 21 October 20122012-10-21T19:00:49Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Tested alpha fragment of beta-galactosidase for complementation with the omega fragment in vivo. A construct consisting of Streptavadin-Linker-Alpha fragment was transformed into BL21(DE3) <i>E.coli</i> cells that naturally express the omega fragment of beta-galactosidase. Quadrant streak plate in the presence of X-gal produced dark blue colonies. These results illustrate alpha-omega complementation <i>in vivo</i>. In vivo complementation indicates the ability of the two fragments to fuse into a functional beta-galactosidase unit, indicating that the split beta-galactosidase reporter system module of the biosensor was constructed and can be implemented successfully.</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><<del class="diffchange diffchange-inline">b</del>>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</<del class="diffchange diffchange-inline">b</del>></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><<ins class="diffchange diffchange-inline">div align="center"</ins>></div></td></tr>
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<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Notably, our data shows that the alpha fragment of beta-galactosidase was still able to complementarily bind to the omega fragment and produce a functional unit while linked to streptavidin, a toxic protein due to its high affinity towards biotin, an essential cofactor for fatty acid synthesis, valine synthesis, and gluconeogenesis. This indicates that the split beta-galactosidase reporter system can still be produced under harsh conditions and within a fusion protein construct. This parallels the conditions that we expect our probe to mature in, given that the beta-galactosidase fragments will also be fused to topoisomerase, which is also a toxic protein that binds DNA. This provides a proof-of-concept for the DNA-based biosensor, given that both modules of the final biosensor design work as expected.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h4>After 6 Hours</h4></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><h4>After 6 Hours</h4></div></td></tr>
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</table>Abhinavmarkus