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


Best, Robert B; Zheng, Wenwei; Borgia, Alessandro; Buholzer, Karin; Borgia, Madeleine B; Hofmann, Hagen; Soranno, Andrea; Nettels, Daniel; Gast, Klaus; Grishaev, Alexander; Schuler, Benjamin (2018). Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science, 361(6405):eaar7101.

Abstract

Riback (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.

Abstract

Riback (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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Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:31 August 2018
Deposited On:23 Nov 2018 14:34
Last Modified:23 Nov 2018 14:35
Publisher:American Association for the Advancement of Science
ISSN:0036-8075
OA Status:Closed
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1126/science.aar7101
PubMed ID:30166459

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