SALT-INDUCED REFOLDING OF MYOGLOBIN AT ACIDIC PH - MOLECULAR-PROPERTIES OF A PARTLY FOLDED INTERMEDIATE
SALT-INDUCED REFOLDING OF MYOGLOBIN AT ACIDIC PH - MOLECULAR-PROPERTIES OF A PARTLY FOLDED INTERMEDIATE
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DOI：
10.1016/0003-9861(92)90458-9
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发表时间：
1992-11-01
影响因子：
3.9
通讯作者：
IRACE, G
中科院分区：
文献类型：
--
作者：
BISMUTO, E;SIRANGELO, I;IRACE, G
用荧光和圆二色谱研究了外源荧光团1，8-苯胺基-1，8-萘磺酸盐在盐诱导下部分折叠的脱脂肌红蛋白和肌红蛋白的分子性质。与部分折叠的蛋白质结合的荧光团的二色性消失表明，在有盐存在的酸性pH下，出现了波动的三级结构(“熔融球状”)。此外，中间体的结构不受血红素的存在的影响，因此表明血红素在肌红蛋白折叠的早期阶段并不是至关重要的。
The molecular properties of the salt-induced partly folded acidic state of apomyoglobin as well as myoglobin were investigated by fluorescence and circular dichroism of the extrinsic fluorophore 1,8-anilinonaphthalenesulfonate. The occurrence of a fluctuating tertiary structure (“molten globule”) at acidic pH in the presence of salt was suggested by the disappearance of the dichroic activity of the fluorophore bound to the partly folded protein. Moreover, the structure of the intermediate is not influenced by the presence of heme, thus suggesting that heme is not crucial in the early stage of myoglobin folding.