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首页> 外文期刊>Biochemistry >A native tertiary interaction stabilizes the A state of cytochrome c.
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A native tertiary interaction stabilizes the A state of cytochrome c.

机译：天然的三级相互作用稳定了细胞色素c的A状态。

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摘要

Certain kinetic intermediates in protein folding are similar to the molten globule, or A state, an equilibrium state of many proteins that is populated under high salt and low pH conditions. Many A states are nearly as compact as native proteins and have native-like secondary structure, but the extent to which nonlocal interactions stabilize the A state is unclear. In this study, thermal denaturation, monitored by circular dichroism, was used to determine the free energy of denaturation of the A state (delta GA<-->D) for Saccharomyces cerevisiae iso-1-ferricytochrome c. Specifically, we examined the wild-type protein, seven variants with amino acid substitutions at the interface between the N- and C-terminal helices, and two variants with mutations at a position close to, but not involved in, the interface. A plot of delta GA<-->D versus delta GN<-->D (the free energy of denaturation of the native state) has a slope near unity, showing that the evolutionarily conserved helix-helix interaction stabilizes the A state to the same degree that it stabilizes the native state.
机译：蛋白质折叠中的某些动力学中间体类似于熔融小球或A状态，这是在高盐和低pH条件下填充的许多蛋白质的平衡状态。许多A状态几乎与天然蛋白质一样紧凑，并具有类似天然的二级结构，但是尚不清楚非本地相互作用稳定A状态的程度。在这项研究中，通过圆二色性监测热变性，用于确定酿酒酵母异-1-铁细胞色素c的A态变性的自由能（δGA -D）。具体来说，我们检查了野生型蛋白，在N和C末端螺旋之间的界面处具有氨基酸取代的七个变体以及在接近但不参与该界面的位置处具有突变的两个变体。 δGA <-> D相对于δGN <-> D（天然状态变性的自由能）的斜率接近于1，表明进化上保守的螺旋-螺旋相互作用将A状态稳定为稳定原生状态的程度相同。

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