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.
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.
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.
| 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 |
| Scopus Subject Areas: | Health Sciences > Multidisciplinary |
| Language: | English |
| Date: | 31 August 2018 |
| Deposited On: | 23 Nov 2018 14:34 |
| Last Modified: | 20 Sep 2023 01:44 |
| 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 |
Best, Robert B