[3P-44] タンパク質二次構造の網羅的予測
The amino acid sequence, which is the primary structure of a protein, has been understood in many species with the decoding of the genome. On the other hand, the tertiary structure, which is directly related to the function, has been revealed only for some proteins due to the difficulty and cost of crystal analysis. To fill this gap in knowledge between primary and tertiary structures, we focused on secondary structures, which are the basic parts of proteins. With recent advances in software, secondary structures can be predicted with high accuracy from amino acid sequences. In this study, we comprehensively predicted the secondary structures of all the proteins of representative species of eukaryotes, bacteria, and archaea, and compared their features. As a result, it was found that eukaryotes have more random coil proteins than bacteria and archaea. Examination of the relationship between phosphorylation and secondary structure showed that random coil proteins are susceptible to phosphorylation. In this study, we used comprehensive prediction to clarify the overall picture of protein structure in living organisms. As a byproduct of the prediction, we have succeeded in extracting proteins with characteristic secondary structure parts.