This title appears in the Scientific Report :
2022
Please use the identifier:
http://dx.doi.org/10.1039/D2RA01478E in citations.
Please use the identifier: http://hdl.handle.net/2128/31688 in citations.
Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?
Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?
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 l...
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Personal Name(s): | Kav, Batuhan |
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Strodel, Birgit (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 |
Published in: | RSC Advances, 12 (2022) 32, S. 20829 - 20837 |
Imprint: |
London
RSC Publishing
2022
|
DOI: |
10.1039/D2RA01478E |
Document Type: |
Journal Article |
Research Program: |
Information Processing in Neuronal Networks |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/31688 in citations.
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. |