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- W2000408345 abstract "The homotetramer of transthyretin (TTR) dissociates into a monomeric amyloidogenic intermediate that self-assembles into amyloid fibrils at low pH. We have performed molecular dynamics simulations of monomeric TTR at neutral and low pH at physiological (310 K) and very elevated temperature (498 K). In the low-pH simulations at both temperatures, one of the two beta-sheets (strands CBEF) becomes disrupted, and alpha-sheet structure forms in the other sheet (strands DAGH). alpha-sheet is formed by alternating alphaL and alphaR residues, and it was first proposed by Pauling and Corey. Overall, the simulations are in agreement with the available experimental observations, including solid-state NMR results for a TTR-peptide amyloid. In addition, they provide a unique explanation for the results of hydrogen exchange experiments of the amyloidogenic intermediate-results that are difficult to explain with beta-structure. We propose that alpha-sheet may represent a key pathological conformation during amyloidogenesis." @default.
- W2000408345 created "2016-06-24" @default.
- W2000408345 creator A5021239442 @default.
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- W2000408345 creator A5049185487 @default.
- W2000408345 date "2004-10-01" @default.
- W2000408345 modified "2023-10-18" @default.
- W2000408345 title "Anatomy of an Amyloidogenic Intermediate" @default.
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- W2000408345 doi "https://doi.org/10.1016/j.str.2004.08.005" @default.
- W2000408345 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15458633" @default.
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