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Team:Imperial College London/Drylab/Enzyme/Simulations
From 2009.igem.org
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In this simulation, all parameters are arbitrary. K1 = 100000, K2 = 1000 and K3 = 0.1. This makes K<sub>M</sub> = 0.01. Furthermore, [E<sub>0</sub>] = 0.01 and [S<sub>0</sub>] = 0.1. The values of K1, K2 and K3 are proportional to their kinetic values [1], while the values of E<sub>0</sub> and S<sub>0</sub> are chosen to ensure a clear graph. | In this simulation, all parameters are arbitrary. K1 = 100000, K2 = 1000 and K3 = 0.1. This makes K<sub>M</sub> = 0.01. Furthermore, [E<sub>0</sub>] = 0.01 and [S<sub>0</sub>] = 0.1. The values of K1, K2 and K3 are proportional to their kinetic values [1], while the values of E<sub>0</sub> and S<sub>0</sub> are chosen to ensure a clear graph. | ||
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Revision as of 21:35, 9 October 2009
Simulation 1: The Generic Graph
This simulation shows the standard enzyme kinetics graph. Concentrations of product, enzyme, substrate, and enzyme-substrate complex over time are shown. Comparisons between the standard enzyme kinetic graph with and without Michaelis-Menten kinetics are made.
In this simulation, all parameters are arbitrary. K1 = 100000, K2 = 1000 and K3 = 0.1. This makes KM = 0.01. Furthermore, [E0] = 0.01 and [S0] = 0.1. The values of K1, K2 and K3 are proportional to their kinetic values [1], while the values of E0 and S0 are chosen to ensure a clear graph.
