Since it is very hard to find relavent kinetic constants ( these constants change with different conditions)we decided to find an order of magnitude for our kinetic constants in certain situations and the rest of the precision we hope to optimize at a certain point in the future.
We looked through many papers and fortunately we managed to find some magnitudes for the dephosphorylation and phosphorylation rate. The smaller the kinetic rates the longer the reaction time.
We also looked into finding the precision and limitations of the fluoresecence reading instrument. The protocol was discussed and preparations were made so that the instrument could be tested tomorrow.
Issues of disscussion :
Are all reactions really elementary ? How accurate is it to assume that the order of magnitude of the kinetic equations is determined by the number of species present in the reactants ?
After some research into paper :
One other math modelling paper looked into modelling the interactions of insulin . The autophosphorylation of (X...), receptor dephosphorylation and degradation of insulin was simply assumed to be first order kinetics.
I did some research into the research of GFP production and found some interesting things:
GFP is a very stable protein. It only denatures after 90 degress celcius and with pH of either below 4 or above 12 . Partial to near renaturation occurs with in minutes following a reversal of denaturing conditions by dialysis or neutralization.
The lower excitation peak of GFP changes with a change in conditions of the environment.
Folding rate of GFP depends upon the concentration of GFP present . The more GFP present the slower the maturation rate. Wild Type GFP maturations takes about 2 hours while GFP mutants maturation time can vary to the degree of 5 mins.
Revision of the Math Model Summary done . To be presented for tomorrows modelling meeting .
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