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Solvent-induced collapse of -synuclein and acid-denatured cytochrome c

¹ Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
² Biomolecular NMR Laboratory, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA

Reprint requests to: Gary J. Pielak, Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; e-mail: gary_pielak{at}unc.edufax: (919) 966-3675.

The effects of solution conditions on protein collapse were studied by measuring the hydrodynamic radii of two unfolded proteins, -synuclein and acid-denatured ferricytochrome c, in dilute solution and in 1 M glucose. The radius of -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 -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 -synuclein, a natively unfolded protein, is collapsed even in dilute solution, but lacks structure.

Keywords: -Synuclein; crowding; cytochrome c; protein folding; protein structure

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