What is TRUE for the sequential model for allosteric enzymes? 1 pts n Pro 1.3 Curriculum sment e Evaluations isite Collection The binding of a substrate disrupts the equilibrium between two states of the enzyme. • The initial molecule of the substrate prevents unproductive colliding between other substrate molecules and the tense form of the enzyme. The rate constant for the binding of a substrate is lower for the last subunit of the enzyme than for the first one. The affinity to the substrate increases due to the influence of neighboring subunits. Cooperativity in the sequential model can only be positive.
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Does the sequential model for allosteric regulation suggest that the tight conformation binds to substrates less tightly?
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Allosteric switching. A substrate binds 100 times as tightly to the $R$ state of an allosteric enzyme as to its T state. Assume that the concerted (MWC) model applies to this enzyme. (See equations for the Concerted Model in the Appendix to Chapter $7 .$ ) (a) By what factor does the binding of one substrate molecule per enzyme molecule alter the ratio of the concentrations of enzyme molecules in the $\mathrm{R}$ and $\mathrm{T}$ states? (b) Suppose that $L,$ the ratio of $[\mathrm{T}]$ to $[\mathrm{R}]$ in the absence of substrate, is $10^{7}$ and that the enzyme contains four binding sites for substrate. What is the ratio of enzyme molecules in the $\mathrm{R}$ state to those in the T state in the presence of saturating amounts of substrate, assuming that the concerted model is obeyed?
You have isolated a dimeric enzyme that contains two identical active sites. The binding of substrate to one active site decreases the substrate affinity of the other active site. Can the concerted model account for this negative cooperativity?
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