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

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dc.creatorSchnabel, Stefan
dc.creatorBachmann, Michael
dc.creatorJanke, Wolfhard
dc.date2009-02-16
dc.date.accessioned2026-07-07T12:42:14Z
dc.date.available2026-07-07T12:42:14Z
dc.descriptionApplying 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.
dc.description3 pages, 2 figures
dc.identifierhttps://arxiv.org/abs/0902.2652
dc.identifierhttp://arxiv.org/abs/0902.2652
dc.identifierNIC series, vol 40, John von Neumann Institute for Computing (NIC), Juelich (2008) 369
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/220005
dc.subjectSoft Condensed Matter
dc.subjectOther Condensed Matter
dc.titleDifferent Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model
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