Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model
arXiv:0710.4927 · doi:10.1063/1.2437204
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.
26 pages, 6 figures
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Cited by in corpus (7)
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- Hierarchies in Nucleation Transitions
- Adsorption of finite polymers in different thermodynamic ensembles
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