Figure 3.

(A) Comparison of measured helix propensity in the wt* peptide and T4 lysozyme (18, 19) (•) and barnase (22) (□).Values given are the change in ΔG of folding relative to alanine. (B) Comparison of measured helix propensity values for the nonpolar amino acids in the RNase T₁ wt* peptide and alanine-based peptides (16) (•) and salt bridge-stabilized peptides (5) (□). Values are the change in ΔG of helix formation relative to alanine. Slopes, intercepts, and correlation coefficients for best-fit linear regressions of the data in A and B are given in Table 2.