Determining the pharmacophore of a group of isosteres

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The discussion centers on the concept of Ki, which is identified as the equilibrium dissociation constant for the binding interaction between an inhibitor and an enzyme. It is explained that Ki is crucial for understanding drug potency, with lower Ki values indicating more potent inhibitors. The relationship between Ki and drug efficacy is emphasized, suggesting that analyzing differences between isosteres could provide insights into their binding characteristics. The biochemical context of Ki is clarified, linking it to the formation of the enzyme-inhibitor complex and its significance in drug design and pharmacology.
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Heres the question:
http://img442.imageshack.us/img442/484/sarr.png
Firstly does anyone know what Ki is? Ionisation constant? I'm guessing its proportional to the drugs potency. I could take a good guess by observing the differences between each isostere but I'm guessing there's some kind of method I should be able to use here.
 
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In biochemistry, KI is the binding constant for an inhibitor. Put more precisely, in the binding interaction between an inhibitor I and enzyme E, which form enzyme-inhibitor complex EI:

E + I <--> EI

KI is the equilibrium dissociation constant for the binding reaction:

K_I = \frac{[E]<i>}{[EI]}</i>

Therefore, more potent inhibitor have lower KI values.
 
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