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. 2012 Sep;140(3):325–339. doi: 10.1085/jgp.201210851

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© 2012 Mason et al.

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Figure 12. — Destabilization of bound peptide analogues by increased luminal to cytosolic K⁺ flux through ryanodine-modified RyR2 channels. (A) Normalized values of the pooled rates of association (1/T_o) for 20 µM ShBP, 85 µM LHBP, 45 µM MHBPI, and 45 µM MHBPII monitored at 50 mV in either symmetrical 210 mM KCl or with 210 mM KCl in the cis chamber and 620 mM KCl in the trans chamber. (B) Normalized values of the pooled rates of dissociation (1/T_B) under the same conditions. Data are plotted as mean ± SEM for between three and eight channels. Each individual value (for 210:210 and 210:620) was normalized to the mean value of the 210:210 data for each peptide. Where differences between values obtained in 210:210 and 210:620 reached statistical significance, these are indicated by asterisks (*, P < 0.05; **, P < 0.01).