Abstract
Disordered Proteins Disordered proteins sample an ensemble of conformations, but it has remained unclear how compact these conformations are in water. Polymer physics relates the radius of gyration ( R g) to solvent quality, with more chain collapse occurring in poorer solvents. Riback et al. developed an analysis scheme that allows them to extract solvent quality and R g from a single small-angle x-ray scattering measurement. Applying this method, they found that even disordered proteins with low net charge and high hydrophobicity remain expanded in water. Science , this issue p. [238][1] [1]: /lookup/doi/10.1126/science.aan5774
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