Two-state folding, folding through intermediates, and metastability in a minimalistic hydrophobic-polar model for proteins.
Within the frame of an effective, coarse-grained hydrophobic-polar protein model, we employ multicanonical Monte Carlo simulations to investigate free-energy landscapes and folding channels of exemplified heteropolymer sequences, which are permutations of each other. Despite the simplicity of the model, the knowledge of the free-energy landscape in dependence of a suitable system order parameter enables us to reveal complex folding characteristics known from real bioproteins and synthetic peptides, such as two-state folding, folding through weakly stable intermediates, and glassy metastability.
Schnabel
Stefan
S
Institut für Theoretische Physik and Centre for Theoretical Sciences (NTZ), Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany. Stefan.Schnabel@itp.uni-leipzig.de
Bachmann
Michael
M
Janke
Wolfhard
W
D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D012997:Solvents / Q000737:chemistry; D055672:Static Electricity
D011506:Proteins; D012997:Solvents