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- W2011056613 abstract "The conformational states sampled by the Alzheimer amyloid β (10-35) (Aβ 10-35) peptide were probed using replica-exchange molecular dynamics (REMD) simulations in explicit solvent. The Aβ 10-35 peptide is a fragment of the full-length Aβ 40/42 peptide that possesses many of the amyloidogenic properties of its full-length counterpart. Under physiological temperature and pressure, our simulations reveal that the Aβ 10-35 peptide does not possess a single unique folded state. Rather, this peptide exists as a mixture of collapsed globular states that remain in rapid dynamic equilibrium with each other. This conformational ensemble is dominated by random coil and bend structures with insignificant presence of an α-helical or β-sheet structure. The 3D structure of Aβ 10-35 is seen to be defined by a salt bridge formed between the side-chains of K28 and D23. This salt bridge is also observed in Aβ fibrils and our simulations suggest that monomeric conformations of Aβ 10-35 contain pre-folded structural motifs that promote rapid aggregation of this peptide." @default.
- W2011056613 created "2016-06-24" @default.
- W2011056613 creator A5034511172 @default.
- W2011056613 creator A5075339260 @default.
- W2011056613 date "2007-02-01" @default.
- W2011056613 modified "2023-10-18" @default.
- W2011056613 title "The Structure of the Alzheimer Amyloid β 10-35 Peptide Probed through Replica-Exchange Molecular Dynamics Simulations in Explicit Solvent" @default.
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- W2011056613 doi "https://doi.org/10.1016/j.jmb.2006.11.015" @default.
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