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• W3113529939 endingPage "106531" @default.
• W3113529939 startingPage "106531" @default.
• W3113529939 abstract "Chemical denaturation is a well-established approach for probing the equilibrium between folded and unfolded states of proteins. We demonstrate applicability of this method to the detection of a small population of a transiently folded structural element in a system that is often considered to be intrinsically fully disordered. The 1HN, 15N, 13Cα, and 13C' chemical shifts of Aβ1-40 and Aβ1-42 peptides and their M35-oxidized variants were monitored as a function of urea concentration and compared to analogous urea titrations of synthetic pentapeptides of homologous sequence. Fitting of the chemical shift titrations yields a 10 ± 1% population for a structured element at the C-terminus of Aβ1-42 that folds with a cooperativity of m = 0.06 kcal/mol·M. The fit also yields the chemical shifts of the folded state and, using a database search, for Aβ1-42 these shifts identified an antiparallel intramolecular β-sheet for residues I32-A42, linked by a type I' β-turn at G37 and G38. The structure is destabilized by oxidation of M35. Paramagnetic relaxation rates and two previously reported weak, medium-range NOE interactions are consistent with this transient β-sheet. Introduction of the requisite A42C mutation and tagging with MTSL resulted in a small stabilization of this β-sheet. Chemical shift analysis suggests a C-terminal β-sheet may be present in Aβ1-40 too, but the turn type at G37 is not type I'. The approach to derive Transient Structure from chemical Denaturation by NMR (TSD-NMR), demonstrated here for Aβ peptides, provides a sensitive tool for identifying the presence of lowly populated, transiently ordered elements in proteins that are considered to be intrinsically disordered, and permits extraction of structural data for such elements." @default.
• W3113529939 created "2021-01-05" @default.
• W3113529939 creator A5024806540 @default.
• W3113529939 creator A5024870980 @default.
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• W3113529939 creator A5049427645 @default.
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• W3113529939 creator A5082289559 @default.
• W3113529939 date "2021-03-01" @default.
• W3113529939 modified "2023-09-26" @default.
• W3113529939 title "A lowly populated, transient β-sheet structure in monomeric Aβ1-42 identified by multinuclear NMR of chemical denaturation" @default.
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• W3113529939 doi "https://doi.org/10.1016/j.bpc.2020.106531" @default.
• W3113529939 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7878406" @default.
• W3113529939 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33453683" @default.
• W3113529939 hasPublicationYear "2021" @default.

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