Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model

Details Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model

2009-02-16

arxiv.org/abs/0902.2652v1

NIC series, vol 40, John von Neumann Institute for Computing (NIC), Juelich (2008) 369

Physics

Condensed Matter

Soft Condensed Matter

3 pages, 2 figures

Scientific paper

Applying multicanonical simulations we investigated folding properties of off-lattice heteropolymers employing a mesoscopic hydrophobic-polar model. We study for various sequences folding channels in the free-energy landscape by comparing the equilibrium conformations with the folded state in terms of an angular overlap parameter. Although all investigated heteropolymer sequences contain the same content of hydrophobic and polar monomers, our analysis of the folding channels reveals a variety of characteristic folding behaviors known from realistic peptides.

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