Team:Imperial College London/Drylab/M1/Protein production/Analysis/Detailed
From 2009.igem.org
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k1 and k2 are the dissociation constants of the forward and reverse reactions. Therefore, we can modify Equation 2 to include the effects of IPTG on the LacI system as follows: | k1 and k2 are the dissociation constants of the forward and reverse reactions. Therefore, we can modify Equation 2 to include the effects of IPTG on the LacI system as follows: | ||
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==Parameters and values== | ==Parameters and values== | ||
{{Imperial/09/TemplateBottom}} | {{Imperial/09/TemplateBottom}} |
Revision as of 12:29, 15 September 2009
In the absence of IPTG
Equation 1: Equation describing the rate of transcription of LacI MRNA (MLacI):
kmlacI is the transcription rate of MlacI (a measure of promoter strength) and dmlacI is the degradation rate. At steady state:
Equation 2: Equation describing the rate of translation of LacI protein (PlacI)
At steady state:
where klacI is the translation rate of lacI protein and dplacI is the degradation rate of PlacI.Equations 3 and 4 describe the transcription and translation of the protein of interest Pout.
Equation 3: Transcription of Pout
Unlike in the previous case, the output promoter is inducible. In the absence of further information, we model the effect of LacI on transcription/ POPS activity with a Hill function, which represses when amounts are above the threshold K, and activates when PlacI amounts fall below threshold. Such assumption can be revised in the light of contradicting experimental data.
At steady state:
Equation 4: Equation describing the rate of translation of protein of interest Pout:
At steady state:
When IPTG is introduced
When IPTG is added into the system, LacI can bind to it, forming an intermediate complex [IPTG-LacI]:
k1 and k2 are the dissociation constants of the forward and reverse reactions. Therefore, we can modify Equation 2 to include the effects of IPTG on the LacI system as follows:
Parameters and values