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• W1993650648 abstract "Protein structure and function depend on a close interplay between intrinsic folding energy landscapes and the chemistry of the protein environment. Osmolytes are small-molecule compounds that can act as chemical chaperones by altering the environment in a cellular context. Despite their importance, detailed studies on the role of these chemical chaperones in modulating structure and dimensions of intrinsically disordered proteins have been limited. Here, we used single-molecule Förster resonance energy transfer to test the counteraction hypothesis of counterbalancing effects between the protecting osmolyte trimethylamine-N-oxide (TMAO) and denaturing osmolyte urea for the case of α-synuclein, a Parkinson’s disease-linked protein whose monomer exhibits significant disorder. The single-molecule experiments, which avoid complications from protein aggregation, do not exhibit clear solvent-induced cooperative protein transitions for these osmolytes, unlike results from previous studies on globular proteins. Our data demonstrate the ability of TMAO and urea to shift α-synuclein structures towards either more compact or expanded average dimensions. Strikingly, the experiments directly reveal that a 2∶1 [urea]∶[TMAO] ratio has a net neutral effect on the protein’s dimensions, a result that holds regardless of the absolute osmolyte concentrations. Our findings shed light on a surprisingly simple aspect of the interplay between urea and TMAO on α-synuclein in the context of intrinsically disordered proteins, with potential implications for the biological roles of such chemical chaperones. The results also highlight the strengths of single-molecule experiments in directly probing the chemical physics of protein structure and disorder in more chemically complex environments." @default.
• W1993650648 created "2016-06-24" @default.
• W1993650648 creator A5021026285 @default.
• W1993650648 creator A5029720502 @default.
• W1993650648 creator A5042463481 @default.
• W1993650648 creator A5077923906 @default.
• W1993650648 date "2012-07-23" @default.
• W1993650648 modified "2023-10-16" @default.
• W1993650648 title "Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape" @default.
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• W1993650648 doi "https://doi.org/10.1073/pnas.1201802109" @default.
• W1993650648 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3497778" @default.
• W1993650648 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22826265" @default.
• W1993650648 hasPublicationYear "2012" @default.
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