Scenarios for protein aggregation: Molecular Dynamics simulations and Bioinformatic Analysis

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dc.creatorDima, Ruxandra I.
dc.creatorTarus, Bogdan
dc.creatorStraub, John E.
dc.creatorThirumalai, D.
dc.date2006-08-29
dc.date.accessioned2026-07-07T07:26:20Z
dc.date.available2026-07-07T07:26:20Z
dc.descriptionThe need to understand the assembly kinetics of fibril formation has become urgent because of the realization that soluble oligomers of amyloidogenic peptides may be even more neurotoxic than the end product, namely, the amyloid fibrils. In order to fully understand the routes to fibril formation one has to characterize the major species in the assembly pathways. The characterization of the energetics and dynamics of oligomers (dimers, trimers etc) is difficult using experiments alone because they undergo large conformational fluctuations. In this context, carefully planned molecular dynamics simulation studies, computations using coarse-grained models, and bioinformatic analysis have given considerable insights into the early events in the route to fibril formation. Here, we describe progress along this direction using examples taken largely from our own work. In this chapter, we focus on aspects of protein aggregation using Abeta-peptides and prion proteins as examples.
dc.description27 pages, 7 figures, book chapter
dc.identifierhttps://arxiv.org/abs/q-bio/0608041
dc.identifierhttp://arxiv.org/abs/q-bio/0608041
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/117038
dc.subjectBiomolecules
dc.titleScenarios for protein aggregation: Molecular Dynamics simulations and Bioinformatic Analysis
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