Fig. 1

Prediction of immunogenicity of human MrgX2 antigen by bioinformatics method. A Prediction of the secondary structure of the human MrgX2 antigen (a) Prediction of the alpha helix of the sequence by the Gamier-Robson method. b Prediction of the alpha helix of the sequence by the Chou-Fasman method. c Prediction of the beta fold of the sequence by the Gamier-Robson method. d The Chou-Fasman method predicts the β-fold of the sequence. e The Gamier-Robson method predicts the rotation angle of the sequence. f The Chou-Fasman method predicts the rotation angle of the sequence. g The Gamier-Robson method predicts the sequence curl. h Eisenberg method predicts alpha-helix hydrophilicity. i Eisenberg method predicts beta-sheet hydrophilicity. j Karplus-Schulz method predicts sequence flexibility. B Kyte-Doolittle method predicts sequence hydrophilicity. C Jameson-Wolf method predicts sequence antigen index. D Emini method predicts sequence surface accessibility. T1 in the red box showed the 286–330 amino acid sequence of human MrgX2 peptide