Quinary interactions with an unfolded state ensemble
Quinary interactions with an unfolded state ensemble
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DOI：
10.1002/pro.3206
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发表时间：
2017-09-01
期刊：
影响因子：
8
通讯作者：
Pielak, Gary J.
中科院分区：
文献类型：
--
作者：
Cohen, Rachel D.;Pielak, Gary J.
Anfinsen的热力学假说指出，蛋白质的天然三维折叠代表具有最低吉布斯自由能的结构。变性自由能的变化可以由折叠状态、未折叠状态或两者的变化引起。最近已经认识到，五元相互作用，仅在细胞中发生的短暂接触，可以通过涉及折叠状态的相互作用来调节蛋白质的稳定性。在这里，我们表明，细胞环境也可以重塑未折叠的状态合奏。
Anfinsen's thermodynamic hypothesis states that the native three-dimensional fold of a protein represents the structure with the lowest Gibbs free energy. Changes in the free energy of denaturation can arise from changes to the folded state, the unfolded state, or both. It has been recently recognized that quinary interactions, transient contacts that take place only in cells, can modulate protein stability through interactions involving the folded state. Here we show that the cellular environment can also remodel the unfolded state ensemble.