Lunasin secondary structure content location from the published literature. (A,B) Secondary structure elements identified by NMR for the recombinant lunasin at pH 3.5 without or with disulfide bond, respectively [36]. (C,D) Secondary structure elements identified by NMR for the recombinant lunasin at pH 6.5 without or with disulfide bond, respectively [36]. (E) Proposed α-helix motif with similarity to chromatin-binding proteins [14]; (F) Structural content observed by molecular dynamics simulations [37]; (G,H) Reduced and oxidized forms of the extended lunasin model analyzed by molecular dynamic studies in water [24], respectively. (I,J) Reduced and oxidized forms from the predicted lunasin model analyzed by molecular dynamic studies in water [24], respectively. (K,L) Reduced and oxidized forms, respectively, from the extended lunasin model analyzed by molecular dynamic studies in mixture of water and TFE [24]. (M,N) Reduced and oxidized forms, respectively, from the predicted lunasin model analyzed by molecular dynamic studies in mixture of water and TFE [24]. Residues in red are α-helix motifs and residues in yellow are from a β-strand.