Detailed folding structures of M-lycotoxin-Hc1a and its mutageneses using 2D HP model

作者：Yan, Shaomin; Wu, Guang^*

来源：Molecular Simulation, 2012, 38(10): 809-822.

DOI：10.1080/08927022.2012.654473

• folding structure
• HP model
• minimal energy
• M-lycotoxin-Hc1a
• mutagenesis
• native state

Although the hydrophobic-polar (HP) model was proposed a decade ago, it applies almost to no real-case study because of its intense computation. In this study, a 2D HP model was applied to study the folding structures of M-lycotoxin-Hc1a, an antimicrobial peptide, in order to get full pictures of its numerous folding structures. The normalised hydrophobicity index was used to convert M-lycotoxin-Hc1a and its six mutageneses into HP sequences, and then the 2D HP model was used to compute all the possible folding structures (3(24) = 282,429,536,481), and finally the normalised hydrophobicity index was used to distinguish the native state. The results showed that M-lycotoxin-Hc1a had 6 and 138 folding structures at their native state with the minimal energy of 213 at pH 2 and pH 7 when glycine served as hydrophobic amino acid. When glycine serves as polar amino acid, M-lycotoxin-Hc1a had 12 and 54 folding structures at their native state with the minimal energy of - 12 and - 13 at pH 2 and pH 7, respectively. This study advanced the knowledge on how to apply the HP model to real-life study, and how the mutageneses influenced the folding structures of M-lycotoxin-Hc1a, their native states and minimal energy at different pH levels.

• 出版日期2012
• 单位广西科学院