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:
影响因子:
--
通讯作者:
Horne WS
中科院分区:
文献类型:
--
作者:
Tavenor NA;Silva KI;Saxena S;Horne WS
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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