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. 2009 Jan;133(1):43–58. doi: 10.1085/jgp.200810004

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© 2009 Zhang et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 3. — Steady-state CPA-blocking affinities of various mutants of E166. (A) CPA dose-dependent inhibition curves of the wild-type (E166) and seven mutants. (B) Relationship between the apparent K_1/2 of CPA and the side chain volume of the amino acid placed at position 166. The K_1/2 value in each mutant was obtained by fitting the dose-dependent curve shown in A to a Langmüir equation (Eq. 1). The x axis represents the side chain volume of amino acids (Zamyatnin, 1972). The number associated with each data point in the plot is the hydrophobicity index of the introduced amino acid (Kyte and Doolittle, 1982). Except for the E166G mutant, all data points were classified into two groups as judged by eyes, and the two groups were enclosed in cyan and magenta circles, respectively. Notice that in comparison with the octanoate affinities shown in Fig. 12, the K_1/2's of E166H, E166Y, E166W, and E166F (red squares) are disproportionally smaller than those of the other mutants.