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. Author manuscript; available in PMC: 2013 Dec 26.
Published in final edited form as: J Am Chem Soc. 2012 Dec 13;134(51):10.1021/ja310585e. doi: 10.1021/ja310585e

Figure 1.

Figure 1

Schematic representations of some of the strategies used by nature to tune the affinity of her receptors. (Top) For many receptors target binding shifts a pre-existing equilibrium between a binding competent state and a non-binding state10. The affinity of the receptor for its target is a function of both the intrinsic affinity of the binding-competent state (Kdint) and the switching equilibrium constant, Ks. (Middle) Mutations at the distal site of the receptor can stabilize the non-binding state thus shifting the dynamic range towards higher target concentrations. (Bottom) The binding of an allosteric inhibitor can also be used to stabilize the non-binding state, reducing Ks and thus raising the overall dissociation constant.