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@ARTICLE{Barz:904306,
author = {Barz, Bogdan and Buell, Alexander K. and Nath, Soumav},
title = {{C}ompact fibril-like structure of amyloid β-peptide
(1–42) monomers},
journal = {Chemical communications},
volume = {57},
number = {7},
issn = {0009-241X},
address = {Cambridge},
publisher = {Soc.},
reportid = {FZJ-2021-05876},
pages = {947 - 950},
year = {2021},
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.},
cin = {IBI-7},
ddc = {540},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {5244 - Information Processing in Neuronal Networks
(POF4-524)},
pid = {G:(DE-HGF)POF4-5244},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:33399148},
UT = {WOS:000612511600025},
doi = {10.1039/D0CC06607A},
url = {https://juser.fz-juelich.de/record/904306},
}