Diversity in Free Energy Landscape of Proteins with the Same Native Topology

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dc.creatorKenzaki, Hiroo
dc.creatorKikuchi, Macoto
dc.date2005-12-09
dc.date2005-12-28
dc.date.accessioned2026-07-07T06:56:26Z
dc.date.available2026-07-07T06:56:26Z
dc.descriptionIn order to elucidate the role of the native state topology and the stability of subdomains in protein folding, we investigate free energy landscape of human lysozyme, which is composed of two subdomains, by Monte Carlo simulations. A realistic lattice model with Go-like interaction is used. We take the relative interaction strength (stability, in other word) of two subdomains as a variable parameter and study the folding process. A variety of folding process is observed and we obtained a phase diagram of folding in terms of temperature and the relative stability. Experimentally-observed diversity in folding process of c-type lysozimes is thus understood as a consequence of the difference in the relative stability of subdomains.
dc.description4 pages, 3 figures
dc.identifierhttps://arxiv.org/abs/q-bio/0512020
dc.identifierhttp://arxiv.org/abs/q-bio/0512020
dc.identifierChem. Phys. Lett. 427 (2006) 414-417
dc.identifierdoi:10.1016/j.cplett.2006.05.112
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/106639
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.subjectBiological Physics
dc.titleDiversity in Free Energy Landscape of Proteins with the Same Native Topology
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