Extended HP model for protein structure prediction.
This paper describes a detailed investigation of a lattice-based HP (hydrophobic-hydrophilic) model for ab initio protein structure prediction (PSP). The outcome of the simplified HP lattice model has high degeneracy, which could mislead the prediction. The HPNX model was proposed to address the degeneracy problem as well as to avoid the conformational deformity with the hydrophilic (P) residues. We have experimentally shown that it is necessary to further improve the existing HPNX model. We have found and solved the critical error of another existing YhHX model. By extracting the significant features from the YhHX for the HPNX model, we have proposed a novel hHPNX model. Hybrid Genetic Algorithm (HGA) has been used to compare the predictability of these models and hHPNX outperformed other models. We preferred 3D face-centered-cube (FCC) lattice configuration to have closest resemblance to the real folded 3D protein.
Hoque
Tamjidul
T
Institute for Integrated and Intelligent Systems, Griffith University, Nathan, QLD, Australia. Tamjidul.Hoque@gmail.com
Chetty
Madhu
M
Sattar
Abdul
A
D000465:Algorithms; D000595:Amino Acid Sequence; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods
D011506:Proteins