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The pathway dynamics were simulated by interconnecting ordinary differential equations describing kinetic behavior of each enzyme in the pathway.
The kinetics of enzymatic and pathway functioning was simulated by interconnecting ODE describing the kinetic behavior of each enzyme in the pathway.
Dynamicity is conferred to the system by interconnecting ordinary differential equations describing kinetic behavior of each enzyme in the pathway, intracellular enzyme levels, and metabolite concentrations, as well as other kinetic parameters.
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They found that they could not understand the behavior of the enzyme without including the effects of the surrounding molecules — water, in particular.
Experiment results also show that the voltammetric behavior of the enzyme electrode depends on the type of room temperature ionic liquid (RTIL) used.
Electrochemical and analytical behavior of the enzyme electrodes was studied by cyclic voltammetry (CV) in the presence or absence of glucose.
Here, using endoglucanase Cel5A from Thermobifida fusca (TfCel5A) as a model, we applied molecular dynamics simulations to explore the dynamic behavior of the enzyme upon substrate binding.
Threonine differs by the terminal oxygen from valine, indicating that additional hydrogen bonding to substrate or reaction products may affect the reaction behavior of the enzyme.
Using a probe with low viscous drag, we found stochastic fluctuation of the rotation rates, a flat energy pathway, and contribution of an inhibited state to the overall behavior of the enzyme.
These flux expressions characterize the behavior of saturable enzyme kinetics and in vivo control mechanisms observed experimentally [23], [31].
In conclusion, we have demonstrated that activation of human HSL against lipid substrates in response to phosphorylation by PKA in vitro is governed by Ser649 and Ser650 and that this activation involves alterations in the kinetic behavior of the enzyme with increases in both maximum turnover rate and S0.5.
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