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. 2009 Apr 29;587(Pt 12):2875–2886. doi: 10.1113/jphysiol.2009.170258

Figure 4. REFER plots for mutants at residues 276 and 1280.

Figure 4

A, selective examples of single channel recordings of the CFTR mutants at 276 and 1280 positions are shown. The top level of each trace is the channel closed state. The values of the equilibrium constant, K, were calculated as a ratio of the areas under the peaks on the all-points histogram (left column) whereas the rate constants were calculated from the dwell-time histograms as ko= 1/τc and kc= 1/τo (two right columns). B, REFER plots for the processes of openings of CFTR mutants at position 276 (A) and position 1280 (B). The type of amino acid is shown in one-letter code near each experimental point. Experimental points shown as mean value ±s.e.m. Slope Φ is shown under the graphs. The exact parameters of the best fit are: for the left graph the slope is 0.938 ± 0.04 (R= 0.997, P= 0.0002), for the right the slope is 0.967 ± 0.09 (R= 0.985, P= 0.0002).