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<p style="text-align:center; font-size:20px;"><font face="verdana">The mathematical model of the proximity dependent ligation involves the following complexes, as defined in the methodology section:</p> | <p style="text-align:center; font-size:20px;"><font face="verdana">The mathematical model of the proximity dependent ligation involves the following complexes, as defined in the methodology section:</p> | ||
<img src="https://static.igem.org/mediawiki/2016/3/33/Modeling_Overview_Chart_2.JPG"><br> | <img src="https://static.igem.org/mediawiki/2016/3/33/Modeling_Overview_Chart_2.JPG"><br> | ||
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+ | <p style="text-align:center; font-size:20px;"><font face="verdana">At chemical equilibrium, the total gibbs free energy of the system will be minimized. The equation for the Gibbs Free Energy of the aptamer-protein interaction is given by: | ||
+ | <i>G =(Go+RTln(Q))</i>, where <i>G</i> denotes the gibbs free energy of the system, <i>Go</i> denotes the free energy change of the reaction under standard conditions (standard gibbs free energy of formation), <i>R</i> denotes the ideal gas constant (8.314 <i>Jk-1 mol-1</i>), T denotes the temperature in Kelvin, and <i>Q</i> denotes the reaction quotient, which is given by <i>Q=[product(s)][reactant(s)]</i>, at the given state. Because aptamer interactions are often defined in terms of dissociation constants (<i>kd</i>), rather than by the standard gibbs free energy of formation (Go), we will define Go in terms of kd to calculate the gibbs free energy change. Because <i>Go = -RTln(1/Kd)</i> at equilibrium, we can use <i>Kd</i> to find <i>Go</i>.</p> | ||
</div> | </div> | ||
Revision as of 21:44, 18 October 2016