Team:UPO-Sevilla/Project/Improving Flip Flop/Modeling/Equations
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<li>γ: Cooperativity of inhibition by the repressor</li> | <li>γ: Cooperativity of inhibition by the repressor</li> | ||
<li>Ki: Binding constant for IPTG to the repressor</li> | <li>Ki: Binding constant for IPTG to the repressor</li> | ||
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<li>η: Maximum number of bound IPTG molecule per repressor</li> | <li>η: Maximum number of bound IPTG molecule per repressor</li> | ||
<li>ktemp: Degradation constant due to the temperature effect</li> | <li>ktemp: Degradation constant due to the temperature effect</li> | ||
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Latest revision as of 22:20, 27 October 2011
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Equations
We define the reactions and the parameters involved in the system.
First we show a summary of the species:
Species:
- Promoter1
- Promoter2
- mRNA1
- mRNA2
- Repressor1/r1
- Repressor2
- Ribosomes
- IPTG
- asRNA
- Protease
Parameters:
- Km : Michaelis constant of transcription
- Kmu: Michaelis constant of translation
- δ: mRNA rate of degradation
- λ: mRNA maximum rate of synthesis
- k: Repressor rate of synthesis
- Kiu: Dissociation constant of repression
- γ: Cooperativity of inhibition by the repressor
- Ki: Binding constant for IPTG to the repressor
- η: Maximum number of bound IPTG molecule per repressor
- ktemp: Degradation constant due to the temperature effect
- kprs: Rate constant for proteolysis kinetic
- kinh: Rate constant for inhibition of translation
- δ3: Degradation rate of asRNA
- kptsa: Degradation rate of Protease
The new equations that complement the basic flip-flop model are:
Proteolysis
protease + repressor1 → protease
Rate law:
Inhibition of translation
asRNA + mRNA1 → RNA1 complex
Rate law: