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

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 Forster 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.

Metadaten
Author details:	Robert B. Best ORCiD, Wenwei Zheng, Alessandro Borgia ORCiD, Karin Buholzer ORCiD, Madeleine B. Borgia ORCiD, Hagen Hofmann, Andrea Soranno, Daniel Nettels, Klaus Gast, Alexander Grishaev ORCiD, Benjamin Schuler ORCiD
DOI:	https://doi.org/10.1126/science.aar7101
ISSN:	0036-8075
ISSN:	1095-9203
Pubmed ID:	https://pubmed.ncbi.nlm.nih.gov/30166459
Title of parent work (English):	Science
Publisher:	American Assoc. for the Advancement of Science
Place of publishing:	Washington
Publication type:	Other
Language:	English
Date of first publication:	2018/08/31
Publication year:	2018
Release date:	2021/10/11
Volume:	361
Issue:	6405
Number of pages:	2
Funding institution:	NIDDK Intramural Research Program of NIH; Arizona State University; Swiss National Science FoundationSwiss National Science Foundation (SNSF)
Organizational units:	Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
DDC classification:	5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Peer review:	Referiert
Publishing method:	Open Access / Bronze Open-Access