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@ARTICLE{Strodel:134965,
author = {Strodel, Birgit and Fitzpatrick, Anthony W. and
Vendruscolo, Michele and Dobson, Christopher M. and Wales,
David J.},
title = {{C}haracterizing the {F}irst {S}teps of {A}myloid
{F}ormation for the ccβ {P}eptide},
journal = {The journal of physical chemistry / B},
volume = {112},
number = {32},
issn = {1520-5207},
address = {Washington, DC},
publisher = {Soc.},
reportid = {FZJ-2013-02980},
pages = {9998 - 10004},
year = {2008},
abstract = {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.},
cin = {ICS-6},
ddc = {530},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000258290000053},
doi = {10.1021/jp801222x},
url = {https://juser.fz-juelich.de/record/134965},
}