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

Robert B. Best; Wenwei Zheng; Alessandro Borgia; Karin Buholzer; Madeleine B. Borgia; Hagen Hofmann; Andrea Soranno; Daniel Nettels; Klaus Gast; Alexander Grishaev; Benjamin Schuler

doi:10.1126/science.aar7101

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

Robert B. Best, Wenwei Zheng, Alessandro Borgia, Karin Buholzer, Madeleine B. Borgia, Hagen Hofmann, Andrea Soranno, Daniel Nettels, Klaus Gast, Alexander Grishaev, Benjamin Schuler

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34 Scopus citations

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 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.

Original language	English
Article number	eaar7101
Journal	Science
Volume	361
Issue number	6405
DOIs	https://doi.org/10.1126/science.aar7101
State	Published - Aug 31 2018

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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 F{\"o}rster 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.",

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AU - Best, Robert B.

AU - Zheng, Wenwei

AU - Borgia, Alessandro

AU - Buholzer, Karin

AU - Borgia, Madeleine B.

AU - Hofmann, Hagen

AU - Soranno, Andrea

AU - Nettels, Daniel

AU - Gast, Klaus

AU - Grishaev, Alexander

AU - Schuler, Benjamin

PY - 2018/8/31

Y1 - 2018/8/31

N2 - 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.

AB - 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.

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

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