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- W2080593071 abstract "We develop a rigorous nonequilibrium thermodynamics for an open system of nonlinear biochemical reactions responsible for cell signal processing. We show that the quality of the biological switch consisting of a phosphorylation-dephosphorylation cycle, such as those in protein kinase cascade, is controlled by the available intracellular free energy from the adenosine triphosphate (ATP) hydrolysis in vivo: $ensuremath{Delta}G={k}_{B}Tmathrm{ln}([mathrm{A}mathrm{T}mathrm{P}]/{K}_{mathrm{e}mathrm{q}}[mathrm{A}mathrm{D}mathrm{P}])$, where ${K}_{mathrm{e}mathrm{q}}$ is the equilibrium constant. The model reveals the correlation between the performance of the switch and the level of $ensuremath{Delta}G$. The result demonstrates the importance of nonequilibrium thermodynamics in analyzing biological information processing, provides its energetic cost, establishes an interplay between signal transduction and energy metabolism in cells, and suggests a biological function for phosphoenergetics in the ubiquitous phosphorylation signaling." @default.
- W2080593071 created "2016-06-24" @default.
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- W2080593071 date "2005-01-18" @default.
- W2080593071 modified "2023-10-18" @default.
- W2080593071 title "Nonequilibrium Thermodynamics and Nonlinear Kinetics in a Cellular Signaling Switch" @default.
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- W2080593071 doi "https://doi.org/10.1103/physrevlett.94.028101" @default.
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