title: Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function.
abstract: We show that a nonspecific hydrophobic energy function can produce protein-like 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.
authors.affiliation: Departamento de Biologia Celular and International Center of Condensed Matter Physics, Universidade de Brasília, Brasília-DF 70910-900, Brazil.
authors.forename: L G
authors.initials: LG
authors.lastname: Garcia
authors.forename: W L
authors.initials: WL
authors.lastname: Treptow
authors.forename: A F
authors.initials: AF
authors.lastname: de Araújo
mesh_terms: D003198:Computer Simulation; D006358:Hot Temperature; D008958:Models, Molecular; D015233:Models, Statistical; D008962:Models, Theoretical; D009010:Monte Carlo Method; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014867:Water
chemical_list: D011506:Proteins; D014867:Water