Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange.
Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange.
复制标题
核糖核酸酶 A 折叠过程中通过酰胺质子交换捕获的结构中间体。
DOI：
10.1021/bi00567a027
复制
发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
Baldwin,RL
中科院分区：
文献类型：
--
作者：
Kim,PS;Baldwin,RL
Peter S. Kim1 和 Robert L. Baldwin* 摘要：在核糖核酸酶 A (RNase A) 的慢折叠物种 (Us) 的折叠反应中，错误脯氨酸异构体的缓慢异构化为低温 (0-10 C) 下的动力学折叠中间体提供了合适的陷阱。已知部分折叠的中间体在脯氨酸异构化发生之前积累，之后形成天然 RNase A。我们已经能够测量对酰胺质子交换的保护，这是由中间体中的结构在折叠路径的不同时间提供的。先前的工作表明，通过在开始重折叠之前标记未折叠蛋白质的酰胺质子，早期的工作表明脯氨酸异构化可以用作 RNase A 折叠中中间体的动力学陷阱。1 结果可总结如下。（1）未折叠的 RNase A 有两类：快速折叠类 UF 和主要（80%）慢速折叠类 Us（Garel &鲍德温,
Peter S. Kim1 and Robert L. Baldwin* abstract: In the folding reaction of the slow-folding species (Us) of ribonuclease A (RNase A), the slow isomerization of wrong proline isomers provides a suitable trap for kinetic folding intermediates at low temperatures (0-10 C). Partly folded intermediates are known to accumulate before proline isomerization takes place, after which native RNase A is formed. We have been able to measure the protection from amide proton exchange which is provided by structure in the intermediates at different times along the folding pathway. Previous work has shown that, by labeling the amide protons of the unfolded protein before initiating refolding, an earlyI^ evious work has shown that proline isomerization can be used as a kinetic trap for intermediates in the folding of RNase A. 1 The results can be summarized as follows.(1) There are two classes of unfolded RNase A: a fast-folding class, UF, and a major (80%) slow-folding class, Us (Garel & Baldwin,