Team:Imperial College London/Templates/ModuleHeader

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| style="font-size:1em;background-color:#ea8828;width:300px;border:20px solid #ea8828;border-top:0px;"| We decided to design a new mechanism for parasite detection - by using the proteases they release. A novel protein bound to the cell surface, with a signalling peptide attached via a protease cleavage site. When the protease comes along, the signal peptide is released, allowing it to activate our signaling module.
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| style="font-size:1em;background-color:#ea8828;width:300px;border:20px solid #ea8828;border-top:0px;"|We decided to design a new mechanism for parasite detection - by using the proteases they release. A novel protein bound to the cell surface, with a signaling peptide attached via a protease cleavage site. When the protease comes along, the signal peptide is released, allowing it to activate our signaling module.
| style="font-size:1em;background-color:#728175;width:300px;border:20px solid #728175;border-top:0px;" valign="top"| To transduce the signal we used a quorum sensing system of a gram positive bacterium. The two component signal transduction system taken from ''S. pneumoniae'' transfers our peptide signal into the cell, activating the fast response module.
| style="font-size:1em;background-color:#728175;width:300px;border:20px solid #728175;border-top:0px;" valign="top"| To transduce the signal we used a quorum sensing system of a gram positive bacterium. The two component signal transduction system taken from ''S. pneumoniae'' transfers our peptide signal into the cell, activating the fast response module.
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| style="font-size:1em;background-color:#e33333;width:300px;border:20px solid #e33333;border-top:0px;" valign="top"| Our fast response mechanism is based around using an enzymatic amplification step acting upon a presynthesised substrate. This greatly reduces the time required for producing a recognisable output, enabling useful field testing kits.
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| style="font-size:1em;background-color:#e33333;width:300px;border:20px solid #e33333;border-top:0px;" valign="top"| Our fast response mechanism is based around using two enzymatic amplification steps involving a transcripted enzyme, a deactivated enzyme and a presynthesised substrate. This greatly reduces the time required for producing a recognisable output, enabling useful field testing kits.
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| style="font-size:1.5em;background-color:#ea8828;width:300px;border:20px solid #ea8828;border-top:0px;" align="right"| <html><a href="https://2010.igem.org/Team:Imperial_College_London/Modules/Detection" style="color:#ffffff;">Learn more...</a></html>
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| style="font-size:1.5em;background-color:#728175;width:300px;border:20px solid #728175;border-top:0px;" align="right"| <html><a href="https://2010.igem.org/Team:Imperial_College_London/Modules/Signaling" style="color:#ffffff;">Learn more...</a></html>
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| style="font-size:1.5em;background-color:#e33333;width:300px;border:20px solid #e33333;border-top:0px;" align="right"| <html><a href="https://2010.igem.org/Team:Imperial_College_London/Modules/Fast_Response" style="color:#ffffff;">Learn more...</a></html>
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Latest revision as of 21:36, 27 October 2010

Detection Module Signaling Module Fast Response Module

We decided to design a new mechanism for parasite detection - by using the proteases they release. A novel protein bound to the cell surface, with a signaling peptide attached via a protease cleavage site. When the protease comes along, the signal peptide is released, allowing it to activate our signaling module. To transduce the signal we used a quorum sensing system of a gram positive bacterium. The two component signal transduction system taken from S. pneumoniae transfers our peptide signal into the cell, activating the fast response module. Our fast response mechanism is based around using two enzymatic amplification steps involving a transcripted enzyme, a deactivated enzyme and a presynthesised substrate. This greatly reduces the time required for producing a recognisable output, enabling useful field testing kits.
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