期刊
SCIENCE
卷 358, 期 6360, 页码 238-241出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan5774
关键词
-
资金
- NIH [GM055694, GM097573, GM103622, 1S10OD018090-01, T32 EB009412, T32 GM007183, T32 GM008720]
- NSF [GRF DGE-1144082, MCB 1516959]
- U.S. Department of Energy [DE-AC02-06CH11357]
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 state of most foldable sequences is expanded; we conjecture that this property was selected by evolution to minimize misfolding and aggregation.
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