Exploring the energy landscape of model proteins: a metric criterion for the determination of dynamical connectivity

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dc.creatorBongini, Lorenzo
dc.creatorLivi, Roberto
dc.creatorPoliti, Antonio
dc.creatorTorcini, Alessandro
dc.date2005-08-25
dc.date.accessioned2026-07-07T06:41:38Z
dc.date.available2026-07-07T06:41:38Z
dc.descriptionA method to reconstruct the energy landscape of small peptides is presented with reference to a 2d off--lattice model. The starting point is a statistical analysis of the configurational distances between generic minima and directly connected pairs (DCP). As the mutual distance of DCP is typically much smaller than that of generic pairs, a metric criterion can be established to identify the great majority of DCP. Advantages and limits of this approach are thoroughly analyzed for three different heteropolymeric chains. A funnel--like structure of the energy landscape is found in all of the three cases, but the escape rates clearly reveal that the native configuration is more easily accessible (and is significantly more stable) for the sequence that is expected to behave as a real protein.
dc.description10 pages, 16 figures, submitted to Physical. Review. E
dc.identifierhttps://arxiv.org/abs/cond-mat/0508610
dc.identifierhttp://arxiv.org/abs/cond-mat/0508610
dc.identifierPhys. Rev. E 72 (2005) 051929
dc.identifierdoi:10.1103/PhysRevE.72.051929
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/101739
dc.subjectSoft Condensed Matter
dc.subjectStatistical Mechanics
dc.subjectBiomolecules
dc.titleExploring the energy landscape of model proteins: a metric criterion for the determination of dynamical connectivity
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