Additional file 1 of Prediction and evolution of B cell epitopes of surface protein in SARS-CoV-2

Additional file 1. Figure S1: Deep analysis of hydrophilicity and hydrophobicity of surface protein of SARS-CoV-2. The online software, ProtScale, was used to predict the hydrophilicity and hydrophobicity of the surface protein deeply. A. The S protein has a maximum score of hydrophobicity, 3.222 at the 7th site, which revealed a strong hydrophobicity; a minimum score of hydrophobicity, -2.589 at the 679th site, which revealed a strong hydrophilicity. The score of hydrophilicity and hydrophobicity on the polypeptide chain of S protein constantly fluctuates, with most of the scores being negative, which revealed the possibility that the protein had bisexual properties on the basis of hydrophilicity. B. The E protein has a maximum score of hydrophobicity, 3.489 at the 21st and the 25th site, which revealed a strong hydrophobicity; a minimum score of hydrophobicity, -1.550 at the 65th site, which revealed a strong hydrophilicity. Most of the scores of the residues being positive, which revealed the possibility that the protein has obvious hydrophobicity. C. The M protein has a maximum score of hydrophobicity, 2.978 at the 84th site, which revealed a strong hydrophobicity; a minimum score of hydrophobicity, -1.956 at the 211th and the 212th site, which revealed a strong hydrophilicity. The scores of hydrophilicity and hydrophobicity on the polypeptide chain of M protein showed large fluctuations, and the number of positive scores and negative scores were similar, the positive scores accounted for the majority, which revealed the possibility that the protein had bisexual properties on the basis of hydrophobicity.