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. 2012 Jul 24;7(7):e41023. doi: 10.1371/journal.pone.0041023

Figure 4. Mutations of the H-bond network behind the selectivity filter.

Figure 4

(I) Mutation sites N629Q (pore loop), F617Y, and Y616F (both: pore helix, P). (II) Inactivation properties of wild-type and mutant hERG channels. Inactivation time courses for the different hERG channels were recorded as shown. A conditioning pulse to +20 mV followed by a 100 ms hyperpolarizing pulse to −100 mV preceded various depolarizing pulses from −90 to +40 mV in 10 mV increments as illustrated by the pulse protocol on top. (III) (A) Exemplary wild-type (WT) hERG current traces elicited by 6 s depolarizing voltage steps from −100 to +40 mV followed by a hyperpolarizing pulse to −140 mV. Respective tail currents are shown enlarged at left. (B) Conductance-voltage relations determined from Boltzmann fits to normalized tail current amplitudes for hERG wild-type and Y616F and N629Q mutant channels. (C) Conductance-voltage relation for the mutant hERG channel F617Y. (D) Inline graphic and k parameters obtained under steady state conditions from the Boltzmann fits for wild-type and mutant channels are summarized at the bottom. *p<0.05 versus wild-type. (IV) (A) Deactivation time courses of wild-type and mutant hERG channels. Tail currents were elicited according to the pulse protocol shown on top. (B) Voltage dependence of mean deactivation time constants (Inline graphic) (n = 4) for the different channels as indicated.