Fig. 7

Reduced AvBD-6 and −12 were structurally different from wild-types AvBDs. a RP-HPLC analysis of AvBD-6 and AvBD-12 reduced by thioredoxin system with various concentrations of thioredoxin (0, 1, and 4 μM). Increased retention time and peak shifts indicate peptide unfolding and exposure of hydrophobic residues caused by thioredoxin treatment. Ten microgram of peptides was completely reduced by treatment with 4 μM thioredoxin. b Circular dichroism spectra of wild-type peptides (solid lines) and reduced peptides (dotted lines). Lines represent the average of six scans (n = 6). Wild-type peptides displayed intracellular β-sheet structure (signal at 205, 216 nm). In contrast, reduced peptides show a signal around 195 nm, indicated random coil structure. Molar ellipticity (θ) = deg.cm².dmol⁻¹