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@ARTICLE{Kav:909157,
author = {Kav, Batuhan and Strodel, Birgit},
title = {{D}oes the inclusion of electronic polarisability lead to a
better modelling of peptide aggregation?},
journal = {RSC Advances},
volume = {12},
number = {32},
issn = {2046-2069},
address = {London},
publisher = {RSC Publishing},
reportid = {FZJ-2022-03036},
pages = {20829 - 20837},
year = {2022},
abstract = {Simulating the process of amyloid aggregation with atomic
detail is a challenging task for various reasons.One of them
is that it is difficult to parametrise a force field such
that all protein states ranging from thefolded through the
unfolded to the aggregated state are represented with the
same level of accuracy.Here, we test whether the
consideration of electronic polarisability improves the
description of thedifferent states of Ab16–22.
Surprisingly, the CHARMM Drude polarisable force field is
found to performworse than its unpolarisable counterpart
CHARMM36m. Sources for this failure of the Drude model
arediscussed.},
cin = {IBI-7},
ddc = {540},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {5244 - Information Processing in Neuronal Networks
(POF4-524)},
pid = {G:(DE-HGF)POF4-5244},
typ = {PUB:(DE-HGF)16},
pubmed = {35919139},
UT = {WOS:000828190700001},
doi = {10.1039/D2RA01478E},
url = {https://juser.fz-juelich.de/record/909157},
}