Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates.
Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates.
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DOI：
10.1371/journal.pone.0015035
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发表时间：
2010-11-30
期刊：
影响因子：
3.7
通讯作者：
Turoverov KK
中科院分区：
文献类型：
--
作者：
Povarova OI;Kuznetsova IM;Turoverov KK
结果表明，低浓度盐酸胍（GdnHCl）可使部分折叠状态的蛋白质聚集，荧光染料1-苯胺基萘-8-磺酸（ANS）与这些聚集体结合，而不是与熔融球状态的蛋白质表面疏水团簇结合。这就是为什么ANS荧光强度的增加通常记录在GdnHCl而不是尿素的蛋白质变性途径中。因此，以前认为在GdnHCl使蛋白质变性的途径中的熔融球状态，实际上，对于某些蛋白质来说，代表部分折叠分子的聚集体。
It was shown that at low concentrations guanidine hydrochloride (GdnHCl) can cause aggregation of proteins in partially folded state and that fluorescent dye 1-anilinonaphthalene-8-sulfonic acid (ANS) binds with these aggregates rather than with hydrophobic clusters on the surface of protein in molten globule state. That is why the increase in ANS fluorescence intensity is often recorded in the pathway of protein denaturation by GdnHCl, but not by urea. So what was previously believed to be the molten globule state in the pathway of protein denaturation by GdnHCl, in reality, for some proteins represents the aggregates of partially folded molecules.
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