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

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

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

Author(s) -

Robert B. Best,

Wenwei Zheng,

Alessandro Borgia,

Karin Buholzer,

Madeleine B. Borgia,

Hagen Hofmann,

Andrea Soranno,

Daniel Nettels,

Klaus Gast,

Alexander Grishaev,

Benjamin Schuler

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aar7101

Subject(s) - förster resonance energy transfer , small angle x ray scattering , scattering , chemical physics , crystallography , compaction , chemistry , materials science , physics , fluorescence , optics , composite material

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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