Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
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DOI：
10.1039/c4sc01094a
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发表时间：
2014-08-01
期刊：
影响因子：
8.4
通讯作者：
Horne WS
中科院分区：
文献类型：
--
作者：
Reinert ZE;Horne WS
蛋白质折叠的热力学是由原子间相互作用和物理力的复杂相互作用决定的。多种非天然的蛋白质样寡聚体具有表现限定的折叠模式的能力。虽然天然蛋白质折叠的能量学研究得很好，但对修饰骨架中控制折叠的力知之甚少。在这里，我们探讨的热力学后果的骨干改变蛋白质折叠，专注于两种类型的化学变化，在不同的结构背景下，一个紧凑的三级折叠。我们的研究结果揭示了对折叠熵的令人惊讶的有利影响，由于天然和非天然骨架的溶剂化差异，伴随着增加未折叠状态系综无序的修饰。
The thermodynamics of protein folding are dictated by a complex interplay of interatomic interactions and physical forces. A variety of unnatural protein-like oligomers have the capacity to manifest defined folding patterns. While the energetics of folding in natural proteins is well studied, little is known about the forces that govern folding in modified backbones. Here, we explore the thermodynamic consequences of backbone alteration on protein folding, focusing on two types of chemical changes made in different structural contexts of a compact tertiary fold. Our results reveal a surprising favorable impact on folding entropy that accompanies modifications that increase disorder in the ensemble of unfolded states, due to differences in the solvation of natural and unnatural backbones.