α-Helices and short peptides connecting α-helices and β-strands can be predicted by using continuous wavelet transform (CWT) under the appropriate dilation after the amino acids of lgca protein are transformed into sequences of hydrophobic values per residue, the prediction accuracy is 76.5% and 85.1% , respectively. We randomly choose 100 proteins, which consist of 25 all-α-helices, 25 β, 25 α+ β and 25α/βproteins from PDBsum database as the test objects, there are 1618 connecting peptides and 747 α-helices. It was found that 1536 connecting peptides can be predicted by CWT and 1308 among them are consistent with the actual structure, the average predicted accuracy is 85.2%. Comparing with the 747 a-helices contained in the 100 proteins, 770 of a-helices can be predicted by this method and 581 of them are accurate, the average predicted accuracy is 75.5% . The result indicates that CWT is an efficient tool to predict the secondary structures of proteins, and has a tremendous development foreground.

Key words: PROTEIN, POLYPEPTIDE, HYDROPHOBILITY, AMINO ACID, SEQUENCE ANALYSIS, wavelet transform