Quantitative and qualitative nature of chemical noise propagation in biochemical reaction networks depend crucially on the topology of the networks. Multisite reversible phosphorylation-dephosphorylation of target proteins is one such recurrently found topology that regulates host of key functions in living cells. Here we analytically calculated the stochasticity in multistep reversible chemical reactions by determining variance of phosphorylated species at the steady state using linear noise approximation to investigate the effect of mass action and Michaelis-Menten kinetics on the noise of phosphorylated species. We probed the dependence of noise on the number of phosphorylation sites and the equilibrium constants of the reaction equilibria to investigate the chemical noise propagation in the multisite phosphorylation chain.
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