Spider silk as archetypal protein elastomer.

Abstract

We present an overview of the physical properties of spider silks, and introduce a model designed to study the energy absorbed by the material as it stretches before breaking. Of particular interest are the inter- and intramolecular hydrogen bonds as well as the role of water in modifying the material properties of silk. A solid understanding of this interaction is of paramount importance for any deeper insights into the mechanical properties of any biomaterial. Here we note that the typical biological material has evolved to function in the fully hydrated elastomeric state. We conclude that silk after its transformation from the hydrated feedstock to the dehydrated fibre state can in fact be analysed in great detail and interpreted as representative of a wide range of elastomeric proteins covering, inter alia, bone, keratins, elastin and collagen.