(Georgia Institute of Technology, 2003-03)
Pokarowski, Piotr; Kolinski, Andrzej; Skolnick, Jeffrey
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 b-type conformations. A sequence has been designed that adopts a native structure, consisting of an antiparallel, six-member Greekkey b-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.