@article {Pokarowski2003, title = {A minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native state}, journal = {Biophysical Journal}, volume = {84}, number = {3}, year = {2003}, month = {mar}, pages = {1518{\textendash}26}, abstract = {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.}, keywords = {Amino Acid Motifs, Computer Simulation, Crystallography, Crystallography: methods, Energy Transfer, Entropy, Mechanical, Models, Molecular, Monte Carlo Method, Peptides, Peptides: chemistry, Protein Conformation, Protein Folding, Protein Structure, Proteins, Proteins: chemistry, Static Electricity, Stress, Tertiary}, issn = {0006-3495}, doi = {10.1016/S0006-3495(03)74964-9}, url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1302725\&tool=pmcentrez\&rendertype=abstract}, author = {Piotr Pokarowski and Andrzej Koli{\'n}ski and Jeffrey Skolnick} }