Journal Article

FZJ-2022-03036

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?

Kav, B.FZJ* ; Strodel, B. (Corresponding author)FZJ*

2022
RSC Publishing London

This record in other databases:      

Please use a persistent id in citations: http://hdl.handle.net/2128/31688  doi:10.1039/D2RA01478E

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.

---

Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2022

---

Database coverage:
; ; ; ; Article Processing Charges ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; Essential Science Indicators ; Fees ; IF < 5 ; JCR ; National-Konsortium ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

---