蛋白质折叠中间体：天然态氢交换
Protein folding intermediates: native-state hydrogen exchange.
作者信息
Bai Y, Sosnick T R, Mayne L, Englander S W
机构信息
Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104-6059, USA.
出版信息
Science. 1995 Jul 14;269(5221):192-7. doi: 10.1126/science.7618079.
Abstract
The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.
摘要
天然细胞色素c在低浓度变性剂中的氢交换行为揭示了一系列亚稳态的、部分展开的形式，这些形式占据了直至完全展开状态的自由能水平。从一种形式到另一种形式的转变是通过一个或多个结构协同单元的展开来实现的。协同单元是完整的ω环或相互稳定的螺旋和环对。通过氢交换检测到的部分展开形式似乎代表了即使在天然条件下也会发生的可逆动态展开反应中的主要中间体，因此可能定义了细胞色素c折叠的主要途径。
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