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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},
}