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. Author manuscript; available in PMC: 2013 Dec 5.
Published in final edited form as: Structure. 2012 Oct 18;20(12):2038–2047. doi: 10.1016/j.str.2012.09.014

Figure 5. The D184N mutation effectively abolishes Ba2+ activation of MthK.

Figure 5

Representative current traces at -100 mV showing MthK channel activation at pH 7.3 with 15 mM Ca2+ at the cytoplasmic side of a bilayer, followed by replacement with a solution containing 100 mM Ba2+ (with no added Ca2+), and then back to 15 mM Ca2+. The top series of traces shows that 100 mM Ba2+ was sufficient to maximally activate wild-type MthK channels (Po = 0.9), whereas no Ba2+ activation was observed with D184N mutant channels (0 openings observed, n=5 different bilayer experiments).