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<h1 style="text-align:center; font-size: 50px;"> <font face= "Poiret One">Conclusion</h2> | <h1 style="text-align:center; font-size: 50px;"> <font face= "Poiret One">Conclusion</h2> | ||
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− | <p style="text-align:center; font-size:20px;"><font face="verdana">In order to confirm that our mathematical model was, indeed, functional, we confirmed | + | <p style="text-align:center; font-size:20px;"><font face="verdana">In order to confirm that our mathematical model was, indeed, functional, we confirmed certain patterns that were to be predicted in the model. For example, a higher <i>kd</i> value would lead to less aptamer-protein complex formation. As expected, this pattern was seen in our model, as a 2-fold decrease in the <i>kd</i> value, generally led to a greater than 10-fold decrease in the protein-aptamer complex that was formed in the model.</p> |
− | <p style="text-align:center; font-size:20px;"><font face="verdana">Our mathematical model was also able to show that lower concentrations of the protein with constant concentrations of aptamer 1, aptamer 2, and the connector would lead to lower overall complex | + | <p style="text-align:center; font-size:20px;"><font face="verdana">Our mathematical model was also able to show that lower concentrations of the protein with constant concentrations of aptamer 1, aptamer 2, and the connector would lead to lower overall complex formation. In other words, when the protein is missing in the system, it is very unlikely for unspecific reactions to take place, and thereby give a false positive signal. As the protein concentration was gradually increased, the number of aptamer-protein complexes increased at an exponential rate, indicating the high sensitivity of the aptamer-protein complex. In other words, only a small amount of the target protein is needed for the large numbers of the complex to form, and give a colorimetric output. </p> |
− | <p style="text-align:center; font-size:20px;"><font face="verdana">To further characterize our system, we would need to modify the concentrations of aptamer 1, aptamer 2, and the connector at a constant protein concentration to find the concentrations of reactants that would optimize the | + | <p style="text-align:center; font-size:20px;"><font face="verdana">To further characterize our system, we would need to modify the concentrations of aptamer 1, aptamer 2, and the connector at a constant protein concentration to find the concentrations of the reactants that would optimize the formation of the aptamer-protein complex in the presence of a protein. Unfortunately, with our oversimplified model, no clear pattern was seen when the concentrations of aptamer 1, aptamer 2, and the connector were modified. We could only observe the general patterns that were seen when the protein concentration was modified. This pattern was also limited to a specific range of protein concentrations (insensible reactant concentrations and gibbs free energy values were seen at several protein concentrations that were tested). A more realistic mathematical model would be needed to quantitatively, rather than qualitatively, discern the complex behavior of the proximity dependent ligation assay.</p> |
Revision as of 23:34, 19 October 2016