Team:Oxford/alternatives to microcompartments
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The resulting relationship suggested that diffusion rate (defined as 1⁄t_end ) was proportional to 1⁄r^2 . In addition to this, we predict that the relative likelihood of a substrate colliding will an enzyme will decrease as the distance between the enzymes’ active sites increase. This will likely follow a 1⁄r^2 relationship if we consider the fact the likelihood of collision is inversely proportional to the fraction of the surface area of a sphere of the distance r that the enzyme occupies. Thus, we predict that the overall rate-distance relationship will take the form: | The resulting relationship suggested that diffusion rate (defined as 1⁄t_end ) was proportional to 1⁄r^2 . In addition to this, we predict that the relative likelihood of a substrate colliding will an enzyme will decrease as the distance between the enzymes’ active sites increase. This will likely follow a 1⁄r^2 relationship if we consider the fact the likelihood of collision is inversely proportional to the fraction of the surface area of a sphere of the distance r that the enzyme occupies. Thus, we predict that the overall rate-distance relationship will take the form: | ||
<br><br> | <br><br> | ||
- | reaction | + | reaction rate ∝ 1⁄(peptide length)^4 |
<br><br> | <br><br> | ||
Thus, the smaller the distance of separation, the higher we expect the rate of reaction to be. However, we must note that this model does not take into consideration stearic hindrances and instabilities that set in when the peptide is made too small. Furthermore, the model is only valid for a minimum radius which is defined as the sum of the two enzyme radii. | Thus, the smaller the distance of separation, the higher we expect the rate of reaction to be. However, we must note that this model does not take into consideration stearic hindrances and instabilities that set in when the peptide is made too small. Furthermore, the model is only valid for a minimum radius which is defined as the sum of the two enzyme radii. |
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