How, when and why proteins collapse: the relation to folding.
How, when and why proteins collapse: the relation to folding.
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DOI：
10.1016/j.sbi.2011.10.005
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发表时间：
2012-02
影响因子：
6.8
通讯作者：
Haran G
中科院分区：
文献类型：
--
作者：
Haran G
未折叠的蛋白质在强变性条件下会高度扩展。然而，当条件更接近天然时，未折叠的蛋白质可能会塌陷成与折叠状态不同的致密球状结构。这种转变类似于均聚物的线圈-球状转变。单分子 FRET 实验特别有利于揭示与折叠状态共存的条件下的折叠状态。在天然未折叠的蛋白质中可以更容易地观察到这种折叠。使用 FRET 和小角散射的时间分辨研究表明，塌缩转变是一个非常快的事件，可能发生在亚微秒的时间尺度上。驱动塌陷的力量可能涉及疏水性和主链相互作用。折叠过程中构型熵的损失使得展开状态与折叠状态相比不太稳定，从而有利于折叠。
Unfolded proteins under strongly-denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the sub-microsecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding.
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影响因子：
5.6
作者：
Hagen, SJ;Eaton, WA
通讯作者：
Eaton, WA
DOI：
10.1073/pnas.0407982102
发表时间：
2005-02-22
影响因子：
11.1
作者：
Kimura, T;Uzawa, T;Fujisawa, T
通讯作者：
Fujisawa, T
影响因子：
5.6
作者：
Dasgupta, Amrita;Udgaonkar, Jayant B.
通讯作者：
Udgaonkar, Jayant B.
影响因子：
3.4
作者：
Hamadani, Kambiz M.;Weiss, Shimon
通讯作者：
Weiss, Shimon
影响因子：
5.6
作者：
Kimura, T;Akiyama, S;Takahashi, S
通讯作者：
Takahashi, S