title: A simple lattice model that exhibits a protein-like cooperative all-or-none folding transition.
abstract: In a recent paper (D. Gront et al., Journal of Chemical Physics, Vol. 115, pp. 1569, 2001) we applied a simple combination of the Replica Exchange Monte Carlo and the Histogram methods in the computational studies of a simplified protein lattice model containing hydrophobic and polar units and sequence-dependent local stiffness. A well-defined, relatively complex Greek-key topology, ground (native) conformations was found; however, the cooperativity of the folding transition was very low. Here we describe a modified minimal model of the same Greek-key motif for which the folding transition is very cooperative and has all the features of the "all-or-none" transition typical of real globular proteins. It is demonstrated that the all-or-none transition arises from the interplay between local stiffness and properly defined tertiary interactions. The tertiary interactions are directional, mimicking the packing preferences seen in proteins. The model properties are compared with other minimal protein-like models, and we argue that the model presented here captures essential physics of protein folding (structurally well-defined protein-like native conformation and cooperative all-or-none folding transition).
authors.affiliation: Faculty of Chemistry, Warsaw University, Pasteura 1, 02-093 Warsaw, Poland. kolinski@chem.uw.edu.pl
authors.forename: Andrzej
authors.initials: A
authors.lastname: Kolinski
authors.forename: Dominik
authors.initials: D
authors.lastname: Gront
authors.forename: Piotr
authors.initials: P
authors.lastname: Pokarowski
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Skolnick
mesh_terms: D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D009010:Monte Carlo Method; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D001704:Biopolymers; D011506:Proteins