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Updated: Jul 16, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Identification of characteristic protein folding channels in a coarse-grained hydrophobic-polar peptide model
Stefan Schnabel1, Michael Bachmann, Wolfhard Janke
1Institut für Theoretische Physik, Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany.
Abstract:
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.
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