Substructural cooperativity and parallel versus sequential events during protein unfolding

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dc.creatorReich, Lothar
dc.creatorWeikl, Thomas R.
dc.date2006-01-28
dc.date.accessioned2026-07-07T07:00:09Z
dc.date.available2026-07-07T07:00:09Z
dc.descriptionAccording to the 'old view', proteins fold along well-defined sequential pathways, whereas the 'new view' sees protein folding as a highly parallel stochastic process on funnel-shaped energy landscapes. We have analyzed parallel and sequential processes on a large number of Molecular Dynamics unfolding trajectories of the protein CI2 at high temperatures. Using rigorous statistical measures, we quantify the degree of sequentiality on two structural levels. The unfolding process is highly parallel on the microstructural level of individual contacts. On a coarser, macrostructural level of contact clusters, characteristic parallel and sequential events emerge. These characteristic events can be understood from loop-closure dependencies between the contact clusters. A correlation analysis of the unfolding times of the contacts reveals a high degree of substructural cooperativity within the contact clusters.
dc.description8 pages, 7 figures (1 figure in color)
dc.identifierhttps://arxiv.org/abs/q-bio/0601046
dc.identifierhttp://arxiv.org/abs/q-bio/0601046
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/107971
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.titleSubstructural cooperativity and parallel versus sequential events during protein unfolding
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