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• W2039414246 endingPage "285221" @default.
• W2039414246 startingPage "285221" @default.
• W2039414246 abstract "The reliable identification of β-aggregating stretches in protein sequences is essential for the development of therapeutic agents for Alzheimer's and Parkinson's diseases, as well as other pathological conditions associated with protein deposition. While the list of aggregation related diseases is growing, it has also been shown that many proteins that are normally well behaved can be induced to aggregate in vitro. This fact suggests the existence of a unified framework that could explain both folding and aggregation. By assuming this universal behaviour, we have recently introduced an algorithm (PASTA: prediction of amyloid structure aggregation), which is based on a sequence-specific energy function derived from the propensity of two residue types to be found paired in neighbouring strands within β-sheets in globular proteins. The algorithm is able to predict the most aggregation-prone portions of several proteins initially unfolded, in excellent agreement with experimental results. Here, we apply the method to a set of proteins which are known to aggregate, but which are natively folded. The quality of the prediction is again very high, corroborating the hypothesis that the amyloid structure is stabilized by the same physico-chemical determinants as those operating in folded proteins." @default.
• W2039414246 created "2016-06-24" @default.
• W2039414246 creator A5049612522 @default.
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• W2039414246 creator A5076985100 @default.
• W2039414246 date "2007-06-25" @default.
• W2039414246 modified "2023-09-25" @default.
• W2039414246 title "Aggregation of natively folded proteins: a theoretical approach" @default.
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• W2039414246 doi "https://doi.org/10.1088/0953-8984/19/28/285221" @default.
• W2039414246 hasPublicationYear "2007" @default.
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