| The Antifreeze protein (AFP) is a special function protein exists in the organisms which live in the cold environment. AFPs can absorb to ice crystal surface to reduce the ice growing temperature without affect the melting point of ice crystals. It is thermal hysteresis phenomenon. In recent years, due to the cross-integration and rapid development of various disciplines, the research of antifreeze proteins has been extended to all aspects of gene sequences, protein sequences, biological experiments and computer simulation. The sequence and structure characteristics of antifreeze proteins were studied by used molecular dynamics simulations and bioinformatics method. And the theoretical results are helpful to understand the mechanism of antifreeze proteins.The protein tertiary structures are determined by the arrangement of amino acids in the peptide chains, which affect the function of antifreeze proteins, so Antifreeze proteins analysis and predicting are necessary for the Antifreeze proteins researching. The negative database was non-antifreeze proteins, they were similar to antifreeze proteins in single peptide component, and the similarity judgment methods were Manhattan distance calculation. The predicting characteristic parameters were dipeptide and pseudo-amino and good predicting result of antifreeze proteins were obtained.Antifreeze proteins from Protein Data Bank (PDB) were classified by the structure and species, and their characteristics were described. We select wild type winter flounder AFP (WFAFP) and four kinds of mutant WFAFP. The molecular dynamics simulations of combination of WFAFP and ice crystal were conducted. Adsorption energy was obtained by theoretical calculation. We funded the wild type WFAFP have higher adsorption energy, and the mutant WFAFP are reduce in different degree. This phenomenon was coincided with WFAFP thermal hysteresis activity change, therefore adsorption energy is an important factor for AFP study. |
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