ABSTRACT
The application of the protein design method based on the HNP model and the relative entropy theory is discussed for four structural classes of real proteins, and the results are compared with that of the HP model. Testing on 190 proteins shows that this method is generally effective for the different structural classes of proteins. Further studies show that the success rate of this method on regular secondary structures is higher than that on the random coil. Additionally, the success rate for different types of amino acids is also analyzed. It is found that the success rate on the hydrophilic residues is higher than those of the other two types. Furthermore, the success rate of this method on the conserved residues is higher than the non-conserved residues. The reasons resulting in the difference of the success rate on different systems were also analyzed. All analyses mentioned above make the foundation for the development and the application of this method in the future.