title: Hydrogen bonding-assisted thermal conduction in β-sheet crystals of spider silk protein.
abstract: Using atomistic simulations, we demonstrate that β-sheet, an essential component of spider silk protein, has a thermal conductivity 1-2 orders of magnitude higher than that of some other protein structures reported in the literature. In contrast to several other nanostructured materials of similar bundled/layered structures (e.g. few-layer graphene and bundled carbon nanotubes), the β-sheet is found to uniquely feature enhanced thermal conductivity with an increased number of constituting units, i.e. β-strands. Phonon analysis identifies inter-β-strand hydrogen bonding as the main contributor to the intriguing phenomenon, which prominently influences the state of phonons in both low- and high-frequency regimes. A thermal resistance model further verifies the critical role of hydrogen bonding in thermal conduction through β-sheet structures.
authors.affiliation: Department of Mechanical and Aerospace Engineering, Utah State University, Logan, UT 84322, USA. ling.liu@usu.edu.
authors.forename: Lin
authors.initials: L
authors.lastname: Zhang
authors.forename: Teli
authors.initials: T
authors.lastname: Chen
authors.forename: Heng
authors.initials: H
authors.lastname: Ban
authors.forename: Ling
authors.initials: L
authors.lastname: Liu
mesh_terms: D000818:Animals; D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry*; D013112:Spiders / Q000737:chemistry; D013814:Thermal Conductivity
chemical_list: D047011:Silk