%0 Journal Article
%A Strodel, Birgit
%A Fitzpatrick, Anthony W.
%A Vendruscolo, Michele
%A Dobson, Christopher M.
%A Wales, David J.
%T Characterizing the First Steps of Amyloid Formation for the ccβ Peptide
%J The journal of physical chemistry  / B
%V 112
%N 32
%@ 1520-5207
%C Washington, DC
%I Soc.
%M FZJ-2013-02980
%P 9998 - 10004
%D 2008
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000258290000053
%R 10.1021/jp801222x
%U https://juser.fz-juelich.de/record/134965