Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms
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 Förster 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.
Fluorescence Resonance Energy Transfer, Small-Angle Neutron Scattering, and Dynamic Light Scattering Study on Interactions of Gemini Surfactants Having Different Spacer Groups with Protein at Various Regions of Binding Isotherms
