Kinetic intermediates in the formation of the cytochrome c molten globule
Kinetic intermediates in the formation of the cytochrome c molten globule
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DOI：
10.1038/nsb1296-1019
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发表时间：
1996-12-01
期刊：
影响因子：
--
通讯作者：
Roder, H
中科院分区：
文献类型：
--
作者：
Colon, W;Roder, H
通过细胞色素 c 的致密酸变性 A 态的平衡和动力学分析，探索了蛋白质折叠中熔球和瞬时中间体之间的关系。氯化物诱导的 A 态形成是一个复杂的反应，其结构中间体类似于天然重折叠条件下发现的结构中间体，包括快速形成的致密态和随后具有相互作用的 N 端和 C 端螺旋的中间体。结合特定螺旋-螺旋堆积相互作用的突变证据，这表明 A 态是晚期折叠中间体的稳定类似物。 L94A 突变阻止了初始折叠后的所有折叠步骤，其平衡状态类似于早期动力学中间体。
The relationship between molten globules and transient intermediates in protein folding has been explored by equilibrium and kinetic analysis of the compact acid-denatured A-state of cytochrome c. The chloride-induced formation of the A-state is a complex reaction with structural intermediates resembling those found under native refolding conditions, including a rapidly formed compact state and a subsequent intermediate with interacting N- and C-terminal helices. Together with mutational evidence for specific helix-helix packing interactions, this shows that the A-state is a stable analogue of a late folding intermediate. The L94A mutation blocks all folding steps after the initial collapse and its equilibrium state resembles early kinetic intermediates.