Difference between revisions of "Team:LambertGA"
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/* Dropdown Content (Hidden by Default) */ | /* Dropdown Content (Hidden by Default) */ | ||
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/* Links inside the dropdown */ | /* Links inside the dropdown */ | ||
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/* Change the background color of the dropdown button when the dropdown content is shown*/ | /* Change the background color of the dropdown button when the dropdown content is shown*/ | ||
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<a href="https://2016.igem.org/Team:LambertGA/Description" class="dropbtn">Project</a> | <a href="https://2016.igem.org/Team:LambertGA/Description" class="dropbtn">Project</a> | ||
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<a class="drplink" style="transition: color 0.5s ease-in-out;" href="https://2016.igem.org/Team:LambertGA/Description">Description</a> | <a class="drplink" style="transition: color 0.5s ease-in-out;" href="https://2016.igem.org/Team:LambertGA/Description">Description</a> | ||
<a class="drplink" style="transition: color 0.5s ease-in-out;" href="https://2016.igem.org/Team:LambertGA/Design">Design</a> | <a class="drplink" style="transition: color 0.5s ease-in-out;" href="https://2016.igem.org/Team:LambertGA/Design">Design</a> | ||
Revision as of 17:47, 15 October 2016
Characterization of Nonlysosomal Proteolysis
The concentration of proteins in a cell is determined by both the amount synthesized and the amount degraded. Thus, protein degradation is a crucial aspect of maintaining intramolecular equilibrium. A class of ATPases known as AAA+ Proteins involves a well-known proteolysis mechanism known as ClpXP in which ClpX unfolds and translocates a tagged protein into a sequestered proteolytic compartment in ClpP.
We devised an inducible genetic construct in which ClpXP will degrade a chromoprotein upon induction. The data will be gathered using a device that can quantify the color of the light reflected by the chromoprotein before and after induction. This will ultimately allow us to measure the relative strength of degradation and further characterize a well-known proteolysis mechanism. Our characterization of ClpXP will serve as a precursor for controlled protein delivery in medicines and subsequently a switch for biosensors.
