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

Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements

(2017) Gustavo Fuertes et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2017) Joshua A. Riback et al.   SCIENCE

Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment

(2016) Wenwei Zheng et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods

(2016) Alessandro Borgia et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

An Adequate Account of Excluded Volume Is Necessary To Infer Compactness and Asphericity of Disordered Proteins by Förster Resonance Energy Transfer

(2015) Jianhui Song et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions

(2015) Herschel M. Watkins et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Small-Angle X-ray Scattering and Single-Molecule FRET Spectroscopy Produce Highly Divergent Views of the Low-Denaturant Unfolded State

(2012) Tae Yeon Yoo et al.   JOURNAL OF MOLECULAR BIOLOGY

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

(2012) H. Hofmann et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

How accurate are polymer models in the analysis of Förster resonance energy transfer experiments on proteins?

(2009) Edward P. O’Brien et al.   JOURNAL OF CHEMICAL PHYSICS