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 linker structure impacts chain dynamics in the coiled-coil supramolecular polymer.
Origins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER Spectroscopy.,Tavenor NA, Silva KI, Saxena S, Horne WS J Phys Chem B. 2014 Jul 24. PMID:25060334[1]
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References
↑ Tavenor NA, Silva KI, Saxena S, Horne WS. Origins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER Spectroscopy. J Phys Chem B. 2014 Jul 24. PMID:25060334 doi:http://dx.doi.org/10.1021/jp505643w
