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• W2126720648 startingPage "12781" @default.
• W2126720648 abstract "The formation of partially unfolded intermediates through conformational excursions out of the native state is the starting point of many diseases involving protein aggregation. Therapeutic strategies often aim to stabilize the native structure and prevent the formation of intermediates that are also cytotoxic in vivo. However, their transient nature and low population makes it difficult to characterize these intermediates. We have probed the backbone dynamics of transthyretin (TTR) over an extended timescale by using NMR spectroscopy and MD simulations. The location and extent of these motions indicates that the backbone flexibility of TTR is a cause of dissociation and destabilization, both of which are responsible for fibril formation. Importantly, approximately 10 % of wild-type TTR exists in an intermediate state, which increased to up to 28 % for pathogenic TTR mutants, for which the formation of the intermediate state is shown to be energetically more favorable compared to the wild type. This result suggests an important role for the intermediates in TTR amyloidosis." @default.
• W2126720648 created "2016-06-24" @default.
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• W2126720648 date "2014-09-22" @default.
• W2126720648 modified "2023-09-24" @default.
• W2126720648 title "Conformational Flexibility Tunes the Propensity of Transthyretin to Form Fibrils Through Non-Native Intermediate States" @default.
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• W2126720648 doi "https://doi.org/10.1002/anie.201407323" @default.
• W2126720648 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25251500" @default.
• W2126720648 hasPublicationYear "2014" @default.
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