TY - JOUR T1 - A minimal proteinlike lattice model: an alpha-helix motif JF - The Journal of Chemical Physics Y1 - 2005 A1 - Piotr Pokarowski A1 - Karol Droste A1 - Andrzej KoliƄski KW - Algorithms KW - Computer Simulation KW - Hydrophobic and Hydrophilic Interactions KW - Protein Folding KW - Protein Structure KW - Proteins KW - Proteins: chemistry KW - Secondary KW - Thermodynamics AB - A simple protein model of a four-helix bundle motif on a face-centered cubic lattice has been studied. Total energy of a conformation includes attractive interactions between hydrophobic residues, repulsive interactions between hydrophobic and polar residues, and a potential that favors helical turns. Using replica exchange Monte Carlo simulations we have estimated a set of parameters for which the native structure is a global minimum of conformational energy. Then we have shown that all the above types of interactions are necessary to guarantee the cooperativity of folding transition and to satisfy the thermodynamic hypothesis. VL - 122 UR - http://www.ncbi.nlm.nih.gov/pubmed/15974798 ER -