Identification of characteristic protein folding channels in a coarse-grained hydrophobic-polar peptide model.
Folding channels and free-energy landscapes of hydrophobic-polar heteropolymers are discussed on the basis of a minimalistic off-lattice coarse-grained model. We investigate how rearrangements of hydrophobic and polar monomers in a heteropolymer sequence lead to completely different folding behaviors. Studying three exemplified sequences with the same content of hydrophobic and polar residues, we can reproduce within this simple model two-state folding, folding through intermediates, as well as metastability.
Schnabel
Stefan
S
Institut für Theoretische Physik, Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany.
Bachmann
Michael
M
Janke
Wolfhard
W
D003198:Computer Simulation; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D010446:Peptide Fragments; D011506:Proteins