Functional expression of a protein in life form is decided by its tertiary structure. In the past few decades, a significant number of studies have been made on this subject. However, the folding rules of a protein still stay unsolved. The challenge is to predict the three-dimensional tertiary structure of a protein from its primary amino acid sequence. We propose a hybrid method combining homology model and the folding approach to predict protein three-dimensional structure from amino acid sequence. The previous researches on folding problem mostly take the HP (Hydrophobic-Polar) model, which is not able to simulate the native structure of proteins. We use a more exquisite model, the sliced lattice model, to approximate the native forms. Another essential factor influencing protein structures is disulfide bonds, which are ignored in the HP model. We use the ant colony optimization algorithm to approximate the folding problem with the constrained disulfide bond on the sliced lattice HP model. We show that the prediction results are better than previous methods by the measurement of RMSD(Root Mean Square Deviation).