FIGURE 7.

Increase in peptide α-helix conformation, ΔX_α, (♦) (measured with CD spectroscopy) and the effective hydrodynamic diameter, d_H, (▴) (measured with DLS) as a function of (A) temperature for C₁₂E₆ and (B) hydrocarbon chain length for β-C_XG₁. A surfactant concentration of ≥10 × CMC and a (KF)_n concentration of 25 μg/ml (which equals 0.14 mM of amino acid residues) were used. The measurements were performed in a 20-mM acetate buffer at pH 4.9. The DLS measurements were performed on solutions of pure surfactant (no peptide added). The solid traces are added as guides for the eye.