Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

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

Published

Author(s)

Robert Best, Alessandro Borgia, Wenwei Zheng, Karin Buholzer, Madeleine Borgia, Hagen Hofmann, Daniel Nettels, Klaus Gast, Alexander Grishaev, Benjamin Schuler

Abstract

The degree of compaction inferred from SAXS experiments by Riback et al. for unfolded proteins in water versus chemical denaturant is highly consistent with the results from 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.
Citation
Science/AAAS

Keywords

SAXS, FRET, IDP, intrinsically disordered proteins, denaturation

Citation

Best, R. , Borgia, A. , Zheng, W. , Buholzer, K. , Borgia, M. , Hofmann, H. , Nettels, D. , Gast, K. , Grishaev, A. and Schuler, B. (2018), Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water", Science/AAAS, [online], https://doi.org/10.1126/science.aar7101 (Accessed April 17, 2024)
Created August 30, 2018, Updated October 13, 2022