TY  - GEN
A1  - Best, Robert B.
A1  - Zheng, Wenwei
A1  - Borgia, Alessandro
A1  - Buholzer, Karin
A1  - Borgia, Madeleine B.
A1  - Hofmann, Hagen
A1  - Soranno, Andrea
A1  - Nettels, Daniel
A1  - Gast, Klaus
A1  - Grishaev, Alexander
A1  - Schuler, Benjamin
T1  - Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
T2  - Science
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 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.
Y1  - 2018
U6  - https://doi.org/10.1126/science.aar7101
SN  - 0036-8075
SN  - 1095-9203
VL  - 361
IS  - 6405
PB  - American Assoc. for the Advancement of Science
CY  - Washington
ER  -