@misc{BestZhengBorgiaetal.2018,
  author    = {Best, Robert B. and Zheng, Wenwei and Borgia, Alessandro and Buholzer, Karin and Borgia, Madeleine B. and Hofmann, Hagen and Soranno, Andrea and Nettels, Daniel and Gast, Klaus and Grishaev, Alexander and Schuler, Benjamin},
  title     = {Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"},
  series = {Science},
  volume    = {361},
  journal   = {Science},
  number    = {6405},
  publisher = {American Assoc. for the Advancement of Science},
  address   = {Washington},
  issn      = {0036-8075},
  doi       = {10.1126/science.aar7101},
  pages     = {2},
  year      = {2018},
  abstract  = {Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction.},
  language  = {en}
}