Figure 3.

Δδ_αH = observed δ_αH − random coil δ_αH for the strand residues ^DP (filled bars), ^DP-TT (open bars) and ^DP-TT₂ (striped bars), 1 mM each in aqueous (9:1 H₂O/D₂O) sodium deuteroacetate buffer, pH 3.8 (uncorrected), 4°C. The reported random coil δ_αH value for lysine was used for ornithine (random coil δ_αH values from ref. 47). No data are shown for the N-terminal residue of each peptide because this terminus is uncapped. For ^DP-TT₂, δ_αH of Thr-17 and Thr-18 could not be unambiguously assigned; the Δδ_αH values shown for these two residues are based on the average of the two observed δ_αH values (4.54 and 4.72 ppm). Chemical shifts were externally referenced to 2,2-dimethyl-2-silapentane-5-sulfonate (DSS).