Team:PennState
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<td style="padding-top:30px; padding-right:30px" valign="top" width="45%"><span style="font-size:18px">Smart Fold Reporter</span> | <td style="padding-top:30px; padding-right:30px" valign="top" width="45%"><span style="font-size:18px">Smart Fold Reporter</span> | ||
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<p> <em>Smart Fold Reporter</em> is the subproject for the first strategy we are trying to express hPPARalpha in <em>E. coli</em>. This project uses altered growth conditions such that this nuclear hormone receptor protein can be successfully epressed and used to transcriptionally report for the presence of phthalates.</p></td> | <p> <em>Smart Fold Reporter</em> is the subproject for the first strategy we are trying to express hPPARalpha in <em>E. coli</em>. This project uses altered growth conditions such that this nuclear hormone receptor protein can be successfully epressed and used to transcriptionally report for the presence of phthalates.</p></td> | ||
<td style="padding-top:30px; padding-right:30px" valign="top" width="45%"><span style="font-size:18px">Nuclear Fusion</span> | <td style="padding-top:30px; padding-right:30px" valign="top" width="45%"><span style="font-size:18px">Nuclear Fusion</span> | ||
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<p> <em> Nuclear Fusion</em> is our second approach to constructing a phthalate detection system in <em> E. coli</em>. In this project we use just the ligand binding domain of hPPARalpha fused to thymidylate synthase (TS). Binding of the phthalate ligand to this chimeric protein activates TS. When this construct is placed in a TS diffident strain, only <em>E. coli</em> in the presence of a hPPARalpha agonist will survive. </p></td> | <p> <em> Nuclear Fusion</em> is our second approach to constructing a phthalate detection system in <em> E. coli</em>. In this project we use just the ligand binding domain of hPPARalpha fused to thymidylate synthase (TS). Binding of the phthalate ligand to this chimeric protein activates TS. When this construct is placed in a TS diffident strain, only <em>E. coli</em> in the presence of a hPPARalpha agonist will survive. </p></td> | ||
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- | + | <td style="padding-top:30px; padding-right:30px" valign="top" width="45%"><span style="font-size:18px">Diauxie Elimination <em>E. coli</em></span> | |
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- | <p>Cellulosic | + | <p><img src="picture here" alt="[img]" style="float:left; margin:5px;"/>Cellulosic biomass is an aboundant and inexpensive energy source that is ideal for bioproduction. A potential problem with the use of biomass for things such as ethanol production is that it is comprised of both glucose and xylose in relitivly equal ratios. Bacteria such as <em>E. coli</em> preferentially use glucose before any other sugar, meaning that the xlyose in the biomass is not utilized.</p> |
<p>In this projcet we attempt to eliminate this phenomenon called diaxie by getting our cells to utilize both sugars at the same time. Solving this problem will lead to more efficent use of cellulosic biomass including moving towards the future of bioproduction: continous processes.</p> | <p>In this projcet we attempt to eliminate this phenomenon called diaxie by getting our cells to utilize both sugars at the same time. Solving this problem will lead to more efficent use of cellulosic biomass including moving towards the future of bioproduction: continous processes.</p> | ||
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Revision as of 19:06, 24 June 2008
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PENN STATE iGEM 2008
Welcome to the Penn State iGEM 2008 team website. We have been working hard at a few different projects for this year's competition. Starting this summer we began working trying to create different types of biosensors that use human nuclear hormone receptors to recognize potentially harmful ligands. We also have been finishing up one of last year's projects which is amied at more reaching efficent bioproduction by altering how E. Coli selects between utilizing 5 and 6 carbon sugars. Please explore our website to find out more about us and our projects! If there are any questions or comments about the information on this site please contact us at gjt5001@psu.edu.
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