Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27Kip1
Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27Kip1
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DOI：
10.1021/bm015502z
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发表时间：
2001-06-01
影响因子：
6.2
通讯作者：
Lumb, KJ
中科院分区：
文献类型：
--
作者：
Flaugh, SL;Lumb, KJ
许多生物活性蛋白在体外热力学理想条件下表现出内在的结构紊乱。然而，在体内，蛋白质存在于拥挤的、热力学上不理想的环境中。我们测试了一个假设，即内在无序的蛋白质在拥挤的条件下采用稳定的结构，其中排除的体积预计会稳定紧凑的天然构象。在大分子拥挤剂的存在下，无论是c-Fos的内在无序的c端激活结构域还是p27的激酶抑制结构域（Kip1），都不会通过圆二色性或荧光光谱的变化来检测到任何显著的构象变化。我们得出的结论是，分子拥挤效应并不一定足以在本质上无序的蛋白质中诱导有序结构。
A number of biologically active proteins exhibit intrinsic structural disorder in vitro under thermodynamically ideal conditions. In vivo, however, proteins exist in a crowded, thermodynamically nonideal environment. We tested the hypothesis that intrinsically disordered proteins adopt stable structure under crowded conditions in which excluded volume is predicted to stabilize compact, native conformations. In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27(Kip1) undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra. We conclude that molecular crowding effects are not necessarily sufficient to induce ordered structure in intrinsically disordered proteins.