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Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/4033

Title: Competition between folding and aggregation in a model for protein solutions
Authors: Maiti, M.
Rao, Madan
Sastry, S.
Keywords: amyloid fibrils
Issue Date: Jun-2010
Publisher: Springer
Citation: European Physical Journal E, 2010, Vol.32, p217
Abstract: We 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.
Description: Restricted Access. An open-access version is available at arXiv.org (one of the alternative locations)
URI: http://hdl.handle.net/2289/4033
ISSN: 1292-895X (Online)
Alternative Location: http://arxiv.org/abs/0910.5340
Copyright: 2010 EDP Sciences /Società Italiana di Fisica/Springer
Appears in Collections:Research Papers (TP)

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