Reversible enzyme-substrate complex formation modifies the region of Turing instability in a reduced two-variable reaction-diffusion model of a metabolic pathway compared to effective kinetics without explicit binding.
Reentrant liquid condensate phase of proteins is stabilized by hydropho- bic and non-ionic interactions.Biophysical Journal, 120(3):28a
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Enzyme-Substrate Complex Formation Modulates Diffusion-Driven Patterning In Metabolic Pathways
Reversible enzyme-substrate complex formation modifies the region of Turing instability in a reduced two-variable reaction-diffusion model of a metabolic pathway compared to effective kinetics without explicit binding.