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

ABSTRACT: A substantial fraction of the proteome is intrinsically disordered, and even well-folded proteins adopt non-native geometries during synthesis, folding, transport, and turnover. Characterization of intrinsically disordered proteins (IDPs) is challenging, in part because of a lack of accurate physical models and the difficulty of interpreting experimental results. We have developed a general method to extract the dimensions and solvent quality (self-interactions) of IDPs from a single small-angle x-ray scattering measurement. We applied this procedure to a variety of IDPs and found that even IDPs with low net charge and high hydrophobicity remain highly expanded in water, contrary to the general expectation that protein-like sequences collapse in water. Our results suggest that the unfolded

SUBMITTER: Riback JA 

PROVIDER: S-EPMC5959285 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature