Origins of structural flexibility in protein-based supramolecular polymers revealed by DEER spectroscopy.

Origins of structural flexibility in protein-based supramolecular polymers revealed by DEER spectroscopy.
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DOI:
10.1021/jp505643w
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发表时间:
2014-08-21
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Horne WS
Horne WS
中科院分区:
其他
文献类型:
--
作者:
Tavenor NA;Silva KI;Saxena S;Horne WS

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仿生超分子聚合物的模块化组装是开发新型软纳米材料的有力技术,而蛋白质折叠是制备此类材料的通用基础。先前的工作证明了密切相关的超分子聚合物的物理性质有显著差异,这些聚合物由构建块组成,其中相同的卷曲形成的肽由两种细微不同的有机连接体(一种是柔性的,另一种是刚性的)中的一种交联。在这里,我们通过分离超分子聚合物链的单个亚基,并通过双电子-电子共振(DEER)光谱探测其结构和构象灵活性来研究这种观察的分子基础。两种不同标记位点的实验自旋-自旋距离分布与分子动力学模拟相结合,可以深入了解连接剂结构如何影响线圈超分子聚合物中的链动力学。
Modular assembly of bio-inspired supramolecular polymers is a powerful technique to develop new soft nanomaterials, and protein folding is a versatile basis for preparing such materials. Previous work demonstrated a significant difference in the physical properties of closely related supramolecular polymers composed of building blocks in which identical coiled-coil-forming peptides are cross-linked by one of two subtly different organic linkers (one flexible and the other rigid). Herein, we investigate the molecular basis for this observation by isolating a single subunit of the supramolecular polymer chain and probing its structure and conformational flexibility by double electron–electron resonance (DEER) spectroscopy. Experimental spin–spin distance distributions for two different labeling sites coupled with molecular dynamics simulations provide insights into how the linker structure impacts chain dynamics in the coiled-coil supramolecular polymer.
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