Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c
Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c
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DOI：
10.1110/ps.24301
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发表时间：
2001-11-01
期刊：
影响因子：
8
通讯作者：
Pielak, GJ
中科院分区：
文献类型：
--
作者：
Morar, AS;Olteanu, A;Pielak, GJ
通过测量稀溶液和1 M葡萄糖中两种未折叠蛋白质，α-突触核蛋白和酸变性铁细胞色素c的流体动力学半径，研究了溶液条件对蛋白质折叠的影响。α-突触核蛋白在稀溶液中的半径小于高度变性状态下的预测半径，并且加入1 M葡萄糖导致进一步的塌陷。圆二色性数据显示α-突触核蛋白在稀溶液和1 M葡萄糖中都缺乏有组织的结构.另一方面，稀溶液中的酸变性细胞色素c的半径与高度变性状态的半径一致，并且1 M葡萄糖诱导塌陷至天然细胞色素c的大小和结构。总之，这些数据表明α-突触核蛋白，一种天然未折叠的蛋白质。即使在稀溶液中也会塌陷，但缺乏结构。
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.