title: Minimal model for studying prion-like folding pathways.
abstract: The Monte Carlo technique is used to simulate the energy landscape and the folding kinetics of a minimal prion-like protein model. We show that the competition between hydrogen-bonding and hydrophobic interactions yields two energetically favored secondary structures, an alpha-helix and a beta-hairpin. Folding simulations indicate that the probability of reaching the alpha-helix form from a denatured random conformation is much higher than the probability of reaching the beta-sheet form, even though the beta-sheet has a lower energy. The existence of a lower energy beta-sheet state gives the possibility for the normal alpha-helix structure to take a structural transformation into the beta-sheet structure under external influences.
authors.affiliation: Department of Physics, University of Waterloo, Waterloo, Ontario, Canada. jeffchen@onsager.uwaterloo.ca
authors.forename: Jeff Z Y
authors.initials: JZ
authors.lastname: Chen
authors.forename: Alexander S
authors.initials: AS
authors.lastname: Lemak
authors.forename: James R
authors.initials: JR
authors.lastname: Lepock
authors.forename: Josh P
authors.initials: JP
authors.lastname: Kemp
mesh_terms: D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D009010:Monte Carlo Method; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D011328:Prions