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@ARTICLE{Schneider:829474,
      author       = {Schneider, Mario and Walta, Stefan and Cadek, Chris and
                      Richtering, Walter and Willbold, Dieter},
      title        = {{F}luorescence correlation spectroscopy reveals a
                      cooperative unfolding of monomeric amyloid-β 42 with a low
                      {G}ibbs free energy},
      journal      = {Scientific reports},
      volume       = {7},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-03172},
      pages        = {2154},
      year         = {2017},
      abstract     = {The amyloid-beta peptide (Aβ) plays a major role in the
                      progression of Alzheimer’s disease. Due to its high
                      toxicity, the 42 amino acid long isoform Aβ42 has become of
                      considerable interest. The Aβ42 monomer is prone to
                      aggregation down to the nanomolar range which makes
                      conventional structural methods such as NMR or X-ray
                      crystallography infeasible. Conformational information,
                      however, will be helpful to understand the different
                      aggregation pathways reported in the literature and will
                      allow to identify potential conditions that favour
                      aggregation-incompetent conformations. In this study, we
                      applied fluorescence correlation spectroscopy (FCS) to
                      investigate the unfolding of Alexa Fluor 488 labelled
                      monomeric Aβ42 using guanidine hydrochloride as a
                      denaturant. We show that our Aβ42 pre-treatment and the
                      low-nanomolar concentrations, typically used for FCS
                      measurements, strongly favour the presence of monomers. Our
                      results reveal that there is an unfolding/folding behaviour
                      of monomeric Aβ42. The existence of a cooperative unfolding
                      curve suggests the presence of structural elements with a
                      Gibbs free energy of unfolding of about 2.8 kcal/mol.},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000401614900012},
      pubmed       = {pmid:28526839},
      doi          = {10.1038/s41598-017-02410-y},
      url          = {https://juser.fz-juelich.de/record/829474},
}