Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
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DOI：
10.1038/nsb0996-782
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发表时间：
1996-09-01
期刊：
影响因子：
--
通讯作者：
Marqusee, S
中科院分区：
文献类型：
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作者：
Chamberlain, AK;Handel, TM;Marqusee, S
尽管普遍观察到单域蛋白以完全合作的方式变性，但在低水平变性剂中核糖核酸酶H的酰胺氢交换表明存在两个部分折叠的物种。这些边缘稳定的物种的结构类似于动态折叠中间体和蛋白质的熔融球状状态。这些数据表明，第一个折叠的区域是蛋白质热力学上最稳定的部分，熔融的球体是在自然状态下处于平衡状态的高自由能构象。
Despite the general observation that single domain proteins denature in a completely cooperative manner, amide hydrogen exchange of ribonuclease H in low levels of denaturant demonstrates the existence of two partially folded species. The structures of these marginally stable species resemble kinetic folding intermediates and the molten globule state of the protein. These data suggest that the first region to fold is the thermodynamically most stable portion of the protein and that the molten globule is a high free energy conformation present at equilibrium in the native state.