%0 Journal Article %J Biophysical Journal %D 2003 %T A minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native state %A Piotr Pokarowski %A Andrzej Koliński %A Jeffrey Skolnick %K Amino Acid Motifs %K Computer Simulation %K Crystallography %K Crystallography: methods %K Energy Transfer %K Entropy %K Mechanical %K Models %K Molecular %K Monte Carlo Method %K Peptides %K Peptides: chemistry %K Protein Conformation %K Protein Folding %K Protein Structure %K Proteins %K Proteins: chemistry %K Static Electricity %K Stress %K Tertiary %X A simple protein model restricted to the face-centered cubic lattice has been studied. The model interaction scheme includes attractive interactions between hydrophobic (H) residues, repulsive interactions between hydrophobic and polar (P) residues, and orientation-dependent P-P interactions. Additionally, there is a potential that favors extended beta-type conformations. A sequence has been designed that adopts a native structure, consisting of an antiparallel, six-member Greek-key beta-barrel with protein-like structural degeneracy. It has been shown that the proposed model is a minimal one, i.e., all the above listed types of interactions are necessary for cooperative (all-or-none) type folding to the native state. Simulations were performed via the Replica Exchange Monte Carlo method and the numerical data analyzed via a multihistogram method. %B Biophysical Journal %V 84 %P 1518–26 %8 mar %G eng %U http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1302725&tool=pmcentrez&rendertype=abstract %R 10.1016/S0006-3495(03)74964-9