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• W2161486437 abstract "The effects of solution conditions on protein collapse were studied by measuring the hydrodynamic radii of two unfolded proteins, alpha-synuclein and acid-denatured ferricytochrome c, in dilute solution and in 1 M glucose. The radius of alpha-synuclein in dilute solution is less than that predicted for a highly denatured state, and adding 1 M glucose causes further collapse. Circular dichroic data show that alpha-synuclein lacks organized structure in both dilute solution and 1 M glucose. On the other hand, the radius of acid-denatured cytochrome c in dilute solution is consistent with that of a highly denatured state, and 1 M glucose induces collapse to the size and structure of native cytochrome c. Taken together, these data show that alpha-synuclein, a natively unfolded protein, is collapsed even in dilute solution, but lacks structure." @default.
• W2161486437 created "2016-06-24" @default.
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• W2161486437 date "2001-11-01" @default.
• W2161486437 modified "2023-10-10" @default.
• W2161486437 title "Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c" @default.
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• W2161486437 doi "https://doi.org/10.1110/ps.24301" @default.
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