Figure 7.

Comparison of interface energetics for PagP β-signal residues with previously reported scales. A, correlation plots generated by comparing the ΔΔG⁰_w,i(φ) (derived from the lipid-facing interface position; top) and the ΔΔG⁰_w,i(π) transfer free energy (derived from the polar protein-facing interface position; bottom) with the Wimley–White interface scale (12). Here, the ΔΔG⁰_w,i(π) scale is derived from the ΔΔG⁰_U→I (W, Y, F, L, I, V, and M) or ΔΔG_U→N observed at the penultimate residue. B, comparison of ΔΔG⁰_w,i(φ) with the whole-protein (7), translocon (9), ΔE₁₂ (13), and dsTβL (11) scales. Linear fits to the correlation are represented as solid lines. Points excluded from the fits are shown as square symbols. Color codes for residues are retained from Fig. 2A for ΔΔG⁰_w,i(φ) and Fig. 3A for ΔΔG⁰_w,i(π). The slope and corresponding regression coefficients are indicated within each panel and are color-coded for the fits to the translocon scale in B.