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- W3048180070 abstract "Aggregation and self-assembly of nuclear coactivator binding domain of CREB-binding protein was studied under different experimental conditions. Single l- or d-enantiomers fold into left- or right-handed helical structures at neutral pH while β-sheet amyloid arrangement occurs under acidic conditions. Mixtures of both enantiomers promote self-assembly into amyloid β-sheet structures highlighting the role of chirality in the formation of thermodynamically more stable racemic β-sheet structures. Fore more information, see the Full Paper by V. Torbeev et al. on page 9889 ff." @default.
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- W3048180070 date "2020-08-06" @default.
- W3048180070 modified "2023-10-16" @default.
- W3048180070 title "Frontispiece: Aggregation and Amyloidogenicity of the Nuclear Coactivator Binding Domain of CREB‐Binding Protein" @default.
- W3048180070 doi "https://doi.org/10.1002/chem.202084471" @default.
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