title: Thermodynamics and kinetics of a Gō proteinlike heteropolymer model with two-state folding characteristics.
abstract: We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar Gō-like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.
authors.affiliation: Institut für Theoretische Physik, Universität Leipzig, Postfach 100 920, D-04009 Leipzig, Germany and Centre for Theoretical Sciences (NTZ), Universität Leipzig, Postfach 100 920, D-04009 Leipzig, Germany.
authors.forename: Anna
authors.initials: A
authors.lastname: Kallias
authors.forename: Michael
authors.initials: M
authors.lastname: Bachmann
authors.forename: Wolfhard
authors.initials: W
authors.lastname: Janke
mesh_terms: D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins