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首页> 外文期刊>Journal of Molecular Biology >Rapid folding and unfolding of Apaf-1 CARD.
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Rapid folding and unfolding of Apaf-1 CARD.

机译：Apaf-1 CARD的快速折叠和展开。

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摘要

Caspase recruitment domains (CARDs) are members of the death domain superfamily and contain six antiparallel helices in an alpha-helical Greek key topology. We have examined the equilibrium and kinetic folding of the CARD of Apaf-1 (apoptotic protease activating factor 1), which consists of 97 amino acid residues, at pH 6 and pH 8. The results showed that an apparent two state equilibrium mechanism is not adequate to describe the folding of Apaf-1 CARD at either pH, suggesting the presence of intermediates in equilibrium unfolding. Interestingly, the results showed that the secondary structure is less stable than the tertiary structure, based on the transition mid-points for unfolding. Single mixing and sequential mixing stopped-flow studies showed that Apaf-1 CARD folds and unfolds rapidly and suggest a folding mechanism that contains parallel channels with two unfolded conformations folding to the native conformation. Kinetic simulations show that a slow folding phase is described by a third conformation in the unfolded ensemble that interconverts with one or both unfolded species. Overall, the native ensemble is formed rapidly upon refolding. This is in contrast to other CARDs in which folding appears to be dominated by formation of kinetic traps.
机译：Caspase募集域（CARD）是死亡域超家族的成员，并在希腊字母α-螺旋拓扑中包含六个反平行螺旋。我们已经检查了Apaf-1（凋亡蛋白酶激活因子1）的CARD的平衡和动力学折叠，它在pH 6和pH 8下由97个氨基酸残基组成。结果表明，明显的两态平衡机制并不明显。足以描述Apaf-1 CARD在任一pH下的折叠，表明在平衡展开中存在中间体。有趣的是，结果显示，基于展开的过渡中点，二级结构的稳定性低于三级结构。单次混合和顺序混合停止流研究表明，Apaf-1 CARD迅速折叠和展开，并提出了一种折叠机制，其中包含带有两个未折叠构象的平行通道，折叠成天然构象。动力学模拟表明，慢速折叠阶段由未折叠的集合体中的第三种构象描述，该构象与一个或两个未折叠的物种互变。总体而言，本地合奏在重新折叠后迅速形成。这与其他CARD折叠形成动态陷阱的情况相反，而其他CARD折叠似乎是主要的。

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