Journal
PHYSICAL REVIEW E
Volume 64, Issue 1, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevE.64.011912
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We show that a nonspecific hydrophobic energy function can produce proteinlike folding behavior of a three-dimensional protein model of 40 monomers in the cubic lattice when the native conformation is chosen judiciously. We confirm that monomer inside/outside segregation is a powerful criterion for the selection of appropriate structures, an idea that was recently proposed with basis on a general theoretical analysis and simulations of much simpler two-dimensional models.
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