dc.contributor.author
Bittracher, Andreas
dc.contributor.author
Moschner, Johann
dc.contributor.author
Koksch, Beate
dc.contributor.author
Netz, Roland
dc.contributor.author
Schütte, Christof
dc.date.accessioned
2021-12-02T08:05:28Z
dc.date.available
2021-12-02T08:05:28Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/32945
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-32671
dc.description.abstract
We demonstrate the application of the transition manifold framework to the late-stage fibrillation process of the NFGAILS peptide, a amyloidogenic fragment of the human islet amyloid polypeptide (hIAPP). This framework formulates machine learning methods for the analysis of multi-scale stochastic systems from short, massively parallel molecular dynamical simulations. We identify key intermediate states and dominant pathways of the process. Furthermore, we identify the optimally timescale-preserving reaction coordinate for the dock-lock process to a fixed pre-formed fibril and show that it exhibits strong correlation with the mean native hydrogen-bond distance. These results pave the way for a comprehensive model reduction and multi-scale analysis of amyloid fibrillation processes.
en
dc.format.extent
12 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
transition manifold analysis
en
dc.subject
NFGAILS amyloid fibrillation
en
dc.subject
locking stage
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
Exploring the locking stage of NFGAILS amyloid fibrillation via transition manifold analysis
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
195
dcterms.bibliographicCitation.doi
10.1140/epjb/s10051-021-00200-0
dcterms.bibliographicCitation.journaltitle
The European Physical Journal B
dcterms.bibliographicCitation.number
10
dcterms.bibliographicCitation.volume
94
dcterms.bibliographicCitation.url
https://doi.org/10.1140/epjb/s10051-021-00200-0
refubium.affiliation
Mathematik und Informatik
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation
Physik
refubium.affiliation.other
Institut für Mathematik
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refubium.affiliation.other
Institut für Chemie und Biochemie
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refubium.funding
Springer Nature DEAL
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin gefördert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
1434-6036
refubium.resourceType.provider
WoS-Alert