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Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/4033
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dc.contributor.authorMaiti, M.-
dc.contributor.authorRao, Madan-
dc.contributor.authorSastry, S.-
dc.date.accessioned2011-04-08T09:18:50Z-
dc.date.available2011-04-08T09:18:50Z-
dc.date.issued2010-06-
dc.identifier.citationEuropean Physical Journal E, 2010, Vol.32, p217en
dc.identifier.issn1292-895X (Online)-
dc.identifier.issn1292-8941-
dc.identifier.urihttp://hdl.handle.net/2289/4033-
dc.descriptionRestricted Access. An open-access version is available at arXiv.org (one of the alternative locations)en
dc.description.abstractWe study the thermodynamic and kinetic consequences of the competition between single-protein folding and protein-protein aggregation using a phenomenological model, in which the proteins can be in the unfolded (U), misfolded (M) or folded (F) states. The phase diagram shows the coexistence between a phase with aggregates of misfolded proteins and a phase of isolated proteins (U or F) in solution. The spinodal at low protein concentrations shows non-monotonic behavior with temperature, with implications for the stability of solutions of folded proteins at low temperatures. We follow the dynamics upon "quenching" from the U-phase (cooling) or the F-phase (heating) to the metastable or unstable part of the phase diagram that results in aggregation. We describe how interesting consequences to the distribution of aggregate size, and growth kinetics arise from the competition between folding and aggregation.en
dc.language.isoenen
dc.publisherSpringeren
dc.relation.urihttp://arxiv.org/abs/0910.5340en
dc.relation.urihttp://dx.doi.org/10.1140/epje/i2010-10621-4en
dc.relation.urihttp://adsabs.harvard.edu/abs/2009arXiv0910.5340Men
dc.rights2010 EDP Sciences /Società Italiana di Fisica/Springeren
dc.subjectamyloid fibrilsen
dc.subjectkineticsen
dc.subjectpeptidesen
dc.subjectdiseaseen
dc.titleCompetition between folding and aggregation in a model for protein solutionsen
dc.typeArticleen
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