title: 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.
authors: Department of Chemistry, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.
authors: Nathan A
authors: NA
authors: Tavenor
authors: K Ishara
authors: KI
authors: Silva
authors: Sunil
authors: S
authors: Saxena
authors: W Seth
authors: WS
authors: Horne
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011108:Polymers / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013113:Spin Labels
chemical_list: D010455:Peptides; D011108:Polymers; D013113:Spin Labels