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001     134965
005     20210129211746.0
024 7 _ |a 10.1021/jp801222x
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024 7 _ |a 1520-6106
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024 7 _ |a 1520-5207
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024 7 _ |a 1089-5647
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024 7 _ |a WOS:000258290000053
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037 _ _ |a FZJ-2013-02980
041 _ _ |a English
082 _ _ |a 530
100 1 _ |a Strodel, Birgit
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245 _ _ |a Characterizing the First Steps of Amyloid Formation for the ccβ Peptide
260 _ _ |a Washington, DC
|c 2008
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336 7 _ |a Journal Article
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520 _ _ |a We employ constant-temperature and replica exchange molecular dynamics to survey the free energy landscape of the ccbeta peptide using a united-atom potential and an implicit solvent representation. Starting from the experimental coiled-coil structure we observe alpha to beta conversion on increasing the temperature, in agreement with experiment. Various beta-sheet trimers are identified as free energy minima, including one that closely resembles the amyloid beta-sheet model previously proposed from experimental data. We characterize two alternative pathways leading to beta-sheets. The first proceeds via direct alpha to beta conversion without dissociation of the trimer, and the second can be classified as a dissociation/reassociation pathway.
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700 1 _ |a Fitzpatrick, Anthony W.
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700 1 _ |a Vendruscolo, Michele
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700 1 _ |a Dobson, Christopher M.
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700 1 _ |a Wales, David J.
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773 _ _ |a 10.1021/jp801222x
|g Vol. 112, no. 32, p. 9998 - 10004
|p 9998 - 10004
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|0 PERI:(DE-600)2006039-7
|t The @journal of physical chemistry / B
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|y 2008
|x 1520-5207
856 4 _ |u http://pubs.acs.org/doi/abs/10.1021/jp801222x
856 4 _ |u https://juser.fz-juelich.de/record/134965/files/FZJ-2013-02980.pdf
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914 1 _ |y 2013
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