Thermodynamics and kinetics of a Gō proteinlike heteropolymer model with two-state folding characteristics.
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.
Kallias
Anna
A
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.
Bachmann
Michael
M
Janke
Wolfhard
W
D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins