In this paper, we find 'good' amino acid sequences that fold to a desired "target" structure as a ground state conformation of lowest accessible Free energy using the modified bond-fluctuation lattice model. In our protein lattice model, bond lengths are set to vary between one and root2 in three dimensions. Our results agree well with the native state energies E-N Comparisons with the "putative native state" (PNS) energy E-PNS and the "hydrophobic zippers" (HZ) energy E-HZ are made. For every sequence, the global energy minimum is found to have multiple degeneracy of conformations, which is the same result as for the constraint-based hydrophobic core construction (CHCC) method. The interior conformations of the ground states are also discussed. [References: 25]
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