Why is silk a tough fibre? Structure analysis of silk proteins elastomericity by small angle x-ray and neutron scattering

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Silks toughness and mechanical tunability does not depend solely on controlled processing but also on the self-organisation of the elastomeric precursor proteins of the silk. It appears that water hydration plays a major role for self-organisation and stability of silk proteins. Recent findings from our lab suggest that the elastomeric nature of silk protein in solution can be derived from a measure of their structural disorder and their relative content of glycine residues. In order to elucidate the mechanisms by which structural disorder and hydration are linked to promote elastomericity in silks we propose to visualise the processes as they occur using small angle scattering (Neutron and X-ray), polarised spectroscopy (FTIR/CD) and thermal analysis (DMA). This will allow us to examine experimentally and analyse in vitro (i) how silk proteins fold and assemble in solution; and, (ii) how hydration affects silk fibres mechanical performances. This project will provide the fundamentals to understand and quantify the dynamics of interactions between large structural proteins and their environment with application to artificial spinning of biopolymer fibres, and chemical control of biological aggregates, such as amyloids.