A Materiomics Approach to Spider Silk: Protein Molecules to Webs |
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Authors: | Anna?Tarakanova Email author" target="_blank">Markus?J?BuehlerEmail author |
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Affiliation: | (1) Laboratory for Atomistic and Molecular Mechanics (LAMM), Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; |
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Abstract: | The exceptional mechanical properties of hierarchical self-assembling silk biopolymers have been extensively studied experimentally
and in computational investigations. A series of recent studies has been conducted to examine structure–function relationships
across different length scales in silk, ranging from atomistic models of protein constituents to the spider web architecture.
Silk is an exemplary natural material because its superior properties stem intrinsically from the synergistic cooperativity
of hierarchically organized components, rather than from the superior properties of the building blocks themselves. It is
composed of beta-sheet nanocrystals interspersed within less orderly amorphous domains, where the underlying molecular structure
is dominated by weak hydrogen bonding. Protein chains are organized into fibrils, which pack together to form threads of a
spider web. In this article we survey multiscale studies spanning length scales from angstroms to centimeters, from the amino
acid sequence defining silk components to an atomistically derived spider web model, with the aim to bridge varying levels
of hierarchy to elucidate the mechanisms by which structure at each composite level contributes to organization and material
phenomena at subsequent levels. The work demonstrates that the web is a highly adapted system where both material and hierarchical
structure across all length scales is critical for its functional properties. |
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