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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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 languageEnglish (US)
Article numbereaar7101
JournalScience
Volume361
Issue number6405
DOIs
StatePublished - Aug 31 2018

ASJC Scopus subject areas

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    Best, R. B., Zheng, W., Borgia, A., Buholzer, K., Borgia, M. B., Hofmann, H., Soranno, A., Nettels, D., Gast, K., Grishaev, A., & Schuler, B. (2018). Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”. Science, 361(6405), [eaar7101]. https://doi.org/10.1126/science.aar7101