The place of inactivated actin and its kinetic predecessor in actin folding-unfolding
The place of inactivated actin and its kinetic predecessor in actin folding-unfolding
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DOI：
10.1021/bi026412x
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发表时间：
2002-11-05
期刊：
影响因子：
2.9
通讯作者：
Turoverov, KK
中科院分区：
文献类型：
--
作者：
Kuznetsova, IM;Stepanenko, OV;Turoverov, KK
研究了不同浓度盐酸胍诱导肌动蛋白展开的动力学。在两个波长记录的色氨酸荧光强度变化的动力学依赖性的参数表示使我们能够检测和表征一种新的基本上未展开的动力学中间体。它的特征表明，这种中间状态是一个预熔融的球状体。结果表明，失活态和完全展开态之间的平衡转变也是一个两步过程，并通过一个本质上未展开的动力学中间体进行。提出了肌动蛋白展开-再折叠的新动力学途径。由此可见，建立的基本未折叠的动力学状态是通路上的中间体，而失活的肌动蛋白是通过部分折叠的蛋白质大分子聚集而稳定的通路外错误折叠状态。
The kinetics of actin unfolding induced by guanidine hydrochloride of different concentrations was studied. The parametric representation of the kinetic dependencies of tryptophan fluorescence intensity changes recorded at two wavelengths allowed us to detect and characterize a new essentially unfolded kinetic intermediate. Its characteristics suggested that this intermediate state is a premolten globule. It was shown that the equilibrium transition between inactivated and completely unfolded states is also a two-step process and proceeds via an essentially unfolded kinetic intermediate. The new kinetic pathway of actin unfolding-refolding was proposed. According to it, the founded essentially unfolded kinetic state is the on-pathway intermediate, while inactivated actin is the off-pathway misfolded state stabilized by aggregation of partially folded macromolecules of protein.