Article
Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes It Soluble.
The Journal of biological chemistry - 11 Dec 2015
Chandrakesan Muralidharan, Bhowmik Debanjan, Sarkar Bidyut, Abhyankar Rajiv, Singh Harwinder, Kallianpur Mamata, Dandekar Sucheta P, Madhu Perunthiruthy K, Maiti Sudipta, Mithu Venus Singh
Abstract excerpt
Aβ self-assembles into parallel cross-β fibrillar aggregates, which is associated with Alzheimer's disease pathology. A central hairpin turn around residues 23-29 is a defining characteristic of Aβ in its aggregated state. Major biophysical properties of Aβ, including this turn, remain unaltered in the central fragment Aβ18-35. Here, we synthesize a single deletion mutant, ΔG25, with the aim of sterically...
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