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

Science. 2018 Aug 31;361(6405):eaar7949. doi: 10.1126/science.aar7949.

Abstract

Best et al claim that we provide no convincing basis to assert that a discrepancy remains between FRET and SAXS results on the dimensions of disordered proteins under physiological conditions. We maintain that a clear discrepancy is apparent in our and other recent publications, including results shown in the Best et al comment. A plausible origin is fluorophore interactions in FRET experiments.

Publication types

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

MeSH terms

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

Substances

  • Water