PROTEIN-FOLDING INTERMEDIATES - NATIVE-STATE HYDROGEN-EXCHANGE
PROTEIN-FOLDING INTERMEDIATES - NATIVE-STATE HYDROGEN-EXCHANGE
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DOI：
10.1126/science.7618079
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发表时间：
1995-07-14
期刊：
影响因子：
56.9
通讯作者：
ENGLANDER, SW
中科院分区：
文献类型：
--
作者：
BAI, YW;SOSNICK, TR;ENGLANDER, SW
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、部分未折叠形式，这些形式占据达到完全未折叠状态的自由能水平。从一种形式到另一种形式的步骤是通过展开一个或多个协作结构单元来完成的。协作单元是整个欧米伽环或相互稳定的完整螺旋和环对。通过氢交换检测到的部分未折叠形式似乎代表了即使在天然条件下也会发生的可逆动态未折叠反应的主要中间体，因此可能定义细胞色素c折叠的主要途径。
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.