Journal Article

FZJ-2021-05876

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Compact fibril-like structure of amyloid β-peptide (1–42) monomers

Barz, B. (Corresponding author)FZJ* ; Buell, A. K. ; Nath, S.

2021
Soc. Cambridge

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Please use a persistent id in citations: doi:10.1039/D0CC06607A

Abstract: Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in most of the individual processes involved in amyloid fibril formation. An important question is whether the monomer can adopt transient fibril-like conformations in solution. Here we use enhanced sampling simulations to study the Aβ42 monomer structural flexibility. We show that the monomer frequently adopts conformations with the N-terminus region structured very similarly to the conformation it adopts inside the fibril. This intrinsic propensity of monomeric Aβ to adopt fibril-like conformations could explain the low free energy barrier for Aβ42 fibril elongation.

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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 2021

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Database coverage:
; Allianz-Lizenz / DFG ; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; Index Chemicus ; JCR ; National-Konsortium ; Nationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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