FORMATION OF A MOLTEN GLOBULE INTERMEDIATE EARLY IN THE KINETIC FOLDING PATHWAY OF APOMYOGLOBIN
FORMATION OF A MOLTEN GLOBULE INTERMEDIATE EARLY IN THE KINETIC FOLDING PATHWAY OF APOMYOGLOBIN
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DOI：
10.1126/science.8235610
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发表时间：
1993-11-05
期刊：
影响因子：
56.9
通讯作者：
WRIGHT, PE
中科院分区：
文献类型：
--
作者：
JENNINGS, PA;WRIGHT, PE
用氢交换脉冲标记和停流圆二色谱确定了去肌红蛋白折叠过程中形成的最早的可检测中间体的结构与先前表征的平衡熔球的结构密切对应。这种紧密的、协同折叠的中间体在不到5毫秒内形成，并包含稳定的氢键二级结构，定位在A、G和H螺旋以及部分B螺旋中。B螺旋的其余部分折叠的时间要慢得多，紧随其后的是C和E螺旋以及CD环。数据表明，在动力学折叠路径上形成了熔融的球状中间体。
Hydrogen exchange pulse labeling and stopped-flow circular dichroism were used to establish that the structure of the earliest detectable intermediate formed during refolding of apomyoglobin corresponds closely to that of a previously characterized equilibrium molten globule. This compact, cooperatively folded intermediate was formed in less than 5 milliseconds and contained stable, hydrogen-bonded secondary structure localized in the A, G, and H helices and part of the B helix. The remainder of the B helix folded on a much slower time scale, followed by the C and E helices and the CD loop. The data indicate that a molten globule intermediate was formed on the kinetic folding pathway.