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- W2079677554 abstract "We employ constant-temperature and replica exchange molecular dynamics to survey the free energy landscape of the ccβ peptide using a united-atom potential and an implicit solvent representation. Starting from the experimental coiled-coil structure we observe α to β conversion on increasing the temperature, in agreement with experiment. Various β-sheet trimers are identified as free energy minima, including one that closely resembles the amyloid β-sheet model previously proposed from experimental data. We characterize two alternative pathways leading to β-sheets. The first proceeds via direct α to β conversion without dissociation of the trimer, and the second can be classified as a dissociation/reassociation pathway." @default.
- W2079677554 created "2016-06-24" @default.
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- W2079677554 date "2008-07-23" @default.
- W2079677554 modified "2023-09-23" @default.
- W2079677554 title "Characterizing the First Steps of Amyloid Formation for the ccβ Peptide" @default.
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- W2079677554 doi "https://doi.org/10.1021/jp801222x" @default.
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