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Kinetic scheme for activation of wild-type, εN436del, and δL42P AChR. AChR activation involves reversible binding of two molecules of agonist (A) to the AChR in the resting, closed state (R), followed by reversible formation of the open state (R*). K1 and K2 are equilibrium dissociation constants of the first and second agonist binding steps; θ indicates the gating equilibrium constant. Values indicated in gray differ markedly from corresponding values for the wild type
