TY  - JOUR
AU  - Kav, Batuhan
AU  - Strodel, Birgit
TI  - Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?
JO  - RSC Advances
VL  - 12
IS  - 32
SN  - 2046-2069
CY  - London
PB  - RSC Publishing
M1  - FZJ-2022-03036
SP  - 20829 - 20837
PY  - 2022
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 35919139
UR  - <Go to ISI:>//WOS:000828190700001
DO  - DOI:10.1039/D2RA01478E
UR  - https://juser.fz-juelich.de/record/909157
ER  -