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. 2011 Jun;137(6):549–562. doi: 10.1085/jgp.201110608

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© 2011 Szollosi et al.

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Figure 4. — Mutations at positions 460 and 1353 do not affect apparent affinity for ATP. (A) Representative traces showing macroscopic current response for WT and T460S to a test [ATP] of 50 µM, bracketed with applications of 2 mM ATP. Different [ATP] were tested several times within one recording. (B) [ATP] dose–response relationships for WT and mutant CFTR channels; currents in test [ATP] were normalized to the average of the currents observed in bracketing segments in the presence of 2 mM ATP. Solid lines show fits of the Michaelis-Menten equation; K_Po values are plotted in the panel. Between 5 and 14 measurements were made for each concentration tested. (C) Estimates of K_rCO for each construct, calculated (see Results) using K_Po from B and P_o;max from Fig. 3 B. (D) Thermodynamic mutant cycle for target pair T460-L1353 built on K_rCO values.