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β | Since there is not much prior knowledge of the solubility difference of the substrate between in the cytoplasm and in the phase, we conservatively assume that π<sup>β</sup><sub>π</sub>=1. As discussed previously, the term 1βπ<sup>βππ<sub>0</sub><sup>1/3</sup></sup> is the orientation factor. The orientation factors of different chemical reactions vary greatly, and the orientation factor data of enzymatic reactions are lacking. But as a proof of concept, we donβt need to be that precise and hence we can roughly estimate the orientation factor to be | + | Since there is not much prior knowledge of the solubility difference of the substrate between in the cytoplasm and in the phase, we conservatively assume that π<sup>β</sup><sub>π</sub>=1. As discussed previously, the term 1βπ<sup>βππ<sub>0</sub><sup>1/3</sup></sup> is the orientation factor. The orientation factors of different chemical reactions vary greatly, and the orientation factor data of enzymatic reactions are lacking. But as a proof of concept, we donβt need to be that precise and hence we can roughly estimate the orientation factor to be 1Γ10<sup>-3</sup>. |
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Revision as of 18:05, 21 October 2019
![](https://static.igem.org/mediawiki/2019/1/15/T--Tsinghua--loading.gif)
β ’. A User-Interface for Our Modeling
User-Interface
interactions
To give you a more intuitive understanding of the phase separation process and the effect of phase separation on the rate of enzymatic reactions, we have made an interactive interface. You can choose the different strengths of interactions between separation elements and different enzyme concentrations to see how the phase separation proceeds and how the rate of the enzymatic reaction changes.
The computation of enzymatic reaction rate changes in the user-interface is based on formula (2.17), which we made some modifications to. First, we assume that every protein cluster forms a real phase, which means ππ=1 for all πβs. Then, we get
![](https://static.igem.org/mediawiki/2019/4/4d/T--Tsinghua--model3form3_1.png)
If we denote by π1 the specific surface area of protein clusters (the ratio of surface area to volume) after phase separation and π0 the specific surface area of protein all protein particles before phase separation, one will find the term π1/30βππ=1π2/3π is exactly equal to π1/π0. We can use this relationship to extend the application of equation (3.1) to the case where the shape of the protein phase is arbitrary (i.e., not necessarily a sphere), just by replacing the term π1/30βππ=1π2/3π with π1/π0. The phase-separated images are two-dimensional, where we can only obtain the ratio of the perimeter to the area of the protein phase (denoted by πΆ1 and πΆ0 after and before the phase separation respectively) rather than the surface area to volume ratio. We can roughly estimate the relationship between the two ratios using the relationship 3πΆ1/πΆ0=2π1/π0. Therefore, we can rewrite (3.1) as
![](https://static.igem.org/mediawiki/2019/a/a8/T--Tsinghua--model3form3_2.png)
The value of πΆ1 can be calculated via image processing programs, while the value of πΆ0 can be inferred from the size of protein particles after scaling to the same scale as the image where we calculate πΆ1.
Since there is not much prior knowledge of the solubility difference of the substrate between in the cytoplasm and in the phase, we conservatively assume that πβπ=1. As discussed previously, the term 1βπβππ01/3 is the orientation factor. The orientation factors of different chemical reactions vary greatly, and the orientation factor data of enzymatic reactions are lacking. But as a proof of concept, we donβt need to be that precise and hence we can roughly estimate the orientation factor to be 1Γ10-3.