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What is the concerted model in the context of allosteric enzymes?
What does the symmetry rule imply about the state of allosteric enzyme subunits in the concerted model?
What role does natural equilibrium play in the conversion of allosteric enzymes from the T state to the R state in the absence of substrate?
How does increasing substrate concentration affect the T state to R state equilibrium in the concerted model?
What is the impact of substrate binding on the trapping of allosteric enzyme subunits in the R state?
How does the concerted model explain the sigmoidal kinetics observed in allosteric enzyme activity?
How do changes in enzyme state and substrate binding as substrate concentration increases lead to a higher reaction velocity?