Question: LO 4 . 2 + 4 . 4 - Q 1 Instead of looking at the kinetics of a drug interacting with an enzyme, you

LO 4.2+4.4-Q1 Instead of looking at the kinetics of a drug interacting with an enzyme, you can use an assay such as a filter binding assay to measure the equilibrium dynamics of the interaction. In the assay results below, you used a constant concentration of a radio-labeled HIV drug Darunavir (1pM) and added an increasing amount of HIV-Protease (enzyme) to your reaction. The results of the experiment are below.
Using the graph:
a. Estimate the \( K_{d}\) for Darunivir. (Note that the radioactivity when the maximum amount of protein, \(50\mu \mathrm{M}\), was added the radioactive signal on the filter paper was \(1*10^{6}\) counts). b. Calculate the \(\Delta G_{\text {bind }}^{o}\) for the interaction between HIV protease and Darunivir at 310 K K
\( y \)
\[
\begin{array}{l}
G-R T \ln (K R)\\
0\\
0
\end{array}
\]
Binding of a drug to a protein is entropically unfavorable (2 molecules bind to form 1 molecule).
Yestertion is VERY favorable. What are two ways that Darunivir-binding could overcome the large entropic unfavourability of binding for a net favorable reaction. Be specific.
Entropic Increase in Binding of the solvent that carraes it
Enthalpic increase in Binding -
The enthalpic encmease cap cone due to string H-bonds cleate cavoialde enthal pac rracractions
d. Sketch a Hill Plot of the Darunivir binding to HIV Protease Data. Indicate what the slope, Xintercept, and Y-intercept would be.
LO 4 . 2 + 4 . 4 - Q 1 Instead of looking at the

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