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The optimization results by conformational space annealing are presented for an off-lattice protein model consisting of hydrophobic and hydrophilic residues in Fibonacci sequences. The ground-state energies found are lower than those reported in the literature. In addition, the ground-state conformations in three dimensions exhibit the important aspect of forming a single hydrophobic core in real proteins. The energy landscape for the population of local minima is also investigated.
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Kim et al. (2005) studied this question.
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