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
refubium.affiliation.other
Institut für Chemie und Biochemie
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
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