Abstract: A biological information processing apparatus predicts a disordered region in a polypeptide. The biological information processing apparatus comprises a prediction target data acquisition unit which acquires amino acid sequence data of a polypeptide of the prediction target; a window level prediction unit which predicts a disordered region at the level of a window sequence with a predetermined window size contained in the amino acid sequence data of the prediction target; and an amino acid residue level prediction unit which predicts a disordered region at the level of each amino acid residue contained in the amino acid sequence data of the prediction target based on the prediction result by the window level prediction unit. With the use of the biological information processing apparatus, the reliability of prediction is improved.

Abstract: A list storing unit stores a plurality of lists, each of which includes a plurality of data and represents a search result of a search in a database. At least a piece of the data in one of the lists is included in another one of the lists. A file name that includes information used for searching data from the database is added to each list. A feature extracting unit extracts features such as similarities and differences between the lists. A feature displaying unit displays extracted features on the screen of a terminal along with the file names. Thus, the features of the lists corresponding to the information are quickly grasped. For example, in a sequence database search, although a data amount included in the lists is huge, similarities among lists can be analyzed in a short time.

Abstract: A prediction method and apparatus for secondary structures of a protein in which accuracy in prediction of a formation of a .beta.-sheet is increased and which can applied to any type of protein including an .alpha.-helix and a .beta.-sheet. Formation of the .alpha.-helix is predicted with respect to each amino acid residue in a sequence of amino acid residues. Then, formation of the .beta.-sheet is predicted with respect to all pairs of residues which were not predicted to form the .alpha.-helix. Results of prediction of the .alpha.-helix and the .beta.-sheet are combined to obtain a result of prediction of the secondary structure of the protein.