Best, R.
, Borgia, A.
, Zheng, W.
, Buholzer, K.
, Borgia, M.
, Hofmann, H.
, Nettels, D.
, Gast, K.
, Grishaev, A.
and Schuler, B.
(2018),
Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water", Science/AAAS, [online], https://doi.org/10.1126/science.aar7101
(Accessed October 15, 2025)
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Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
Published
Author(s)
Robert Best, Alessandro Borgia, Wenwei Zheng, Karin Buholzer, Madeleine Borgia, Hagen Hofmann, Daniel Nettels, Klaus Gast, , Benjamin Schuler
Abstract
The degree of compaction inferred from SAXS experiments by Riback et al. for unfolded proteins in water versus chemical denaturant is highly consistent with the results from 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.Citation
Science/AAAS
Pub Type
Journals
Download Paper
Keywords
SAXS, FRET, IDP, intrinsically disordered proteins, denaturation
Citation
Issues
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Created August 30, 2018, Updated October 13, 2022