Figure 1.

Analysis of the amino acid sequences of helices α-2b and α-3 of Cry1Ab. (A) Alignment of the amino acid sequence of regions containing helices α-2b and α-3 from Cry toxins, which have available structures. The α-helix structures observed in their three-dimensional structures are shown in gray. (B) Prediction of the secondary structure of the Cry1Ab hairpin regions among all α-helices of domain I, by using the i-TASSER server. H, α-helix; S, β-strand; C, coil (C) Prediction of the secondary structure of the coiled toxin regions between helices α-2b and α-3 of different Cry toxins by using the i-TASSER server, showing high probability to form an extended helix α-3. H, α-helix; S, β-strand; C, coil.