Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.
Science
; 358(6360): 238-241, 2017 10 13.
Article
em En
| MEDLINE
| ID: mdl-29026044
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 state of most foldable sequences is expanded; we conjecture that this property was selected by evolution to minimize misfolding and aggregation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Difração de Raios X
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Água
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Dobramento de Proteína
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Espalhamento a Baixo Ângulo
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Proteínas Intrinsicamente Desordenadas
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article