Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"

Science. 2018 Aug 31;361(6405):eaau8230. doi: 10.1126/science.aau8230.


Editors at Science requested our input on the above discussion (comment by Best et al and response by Riback et al) because both sets of authors use our data from Fuertes et al (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins
  • Protein Conformation
  • Scattering, Small Angle*
  • Water
  • X-Ray Diffraction*


  • Intrinsically Disordered Proteins
  • Water