Abstract: The residual amino acid sequences of CHI of Arabidopsis thaliana, Pyrus pyrifolia cultivar Meirensu, Malus hybrid cultivar, Prunus persica ,Vitis vinifera, Fragaria×ananassa, Citrus sinensis, Zea mays were adopted from GeneBank. The composition of the residual amino acid sequences, leader peptide, signal peptide, transmembrane topological structure, hydrophobicity / hydrophilicity, the secondary structure, the tertiary structure and functional domains of the proteins were predicted and analyzed. The results showed that CHI of 8 plant species was a nontransmembrane protein without leader peptide and signal peptide. It was supposed that CHI was positioned to the cell matrix to function directly, the polypeptide chain was generally hydrophobic. There were 4 types of secondary structure including αhelix, βturn, random coil and extended stand. Except for that the irregular coil was the main secondary motif of Prunus persica, αhelix was the most principal structure motif of the rest 7 plant species. All the eight plant species possessed a chalcone isomerase active site.