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


ABSTRACT: 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.

SUBMITTER: Tavenor NA 

PROVIDER: S-EPMC4141697 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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

Tavenor Nathan A NA   Silva K Ishara KI   Saxena Sunil S   Horne W Seth WS  

The journal of physical chemistry. B 20140811 33


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 inve  ...[more]

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