Figure 3.
Figure 3. KcsA E71A functional properties are preserved after transfer from NABBs to BLMs. (A) Representative single-channel traces of KcsA E71A transferred from 1K-NABBs to BLMs in the absence (top) or presence (bottom) of 5 µM BaCl2 added to the trans chamber. The electrophysiology recording conditions were 100 mM of symmetric K+ across the BLM (Vm = +100 mV; low-pass filter at 1 kHz). (B) Single-channel I-V plot of KcsA E71A transferred from NABBs. (C) Open probability (Po) of the transferred channel as a function of voltage. The change in Po in the case of Ba2+ block was fit to the equation:Po(V)=11+BK0⋅e−zFVRT,where B is the blocker concentration (5 µM), K0 is the apparent blocker affinity at 0 mV, and z is the voltage dependence. The fit values for K0 and z were 48.2 ± 5.6 µM and 0.54 ± 0.02, respectively. Symbols represent averages ± SD from three separate experiments.
KcsA E71A functional properties are preserved after transfer from NABBs to BLMs. (A) Representative single-channel traces of KcsA E71A transferred from 1K-NABBs to BLMs in the absence (top) or presence (bottom) of 5 µM BaCl2 added to the trans chamber. The electrophysiology recording conditions were 100 mM of symmetric K+ across the BLM (Vm = +100 mV; low-pass filter at 1 kHz). (B) Single-channel I-V plot of KcsA E71A transferred from NABBs. (C) Open probability (Po) of the transferred channel as a function of voltage. The change in Po in the case of Ba2+ block was fit to the equation:
Po(V)=11+BK0⋅e−zFVRT,
where B is the blocker concentration (5 µM), K0 is the apparent blocker affinity at 0 mV, and z is the voltage dependence. The fit values for K0 and z were 48.2 ± 5.6 µM and 0.54 ± 0.02, respectively. Symbols represent averages ± SD from three separate experiments.
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