Concentration dependence of silk proteins’ structure and dynamics in solution

DOI

The formation of silk fibres in both spiders and silkworms is characterized by a controlled conversion of short range ordered structures in solution into long range ordered beta-sheet rich structures in the final fibre (1). The dynamics of the water and proteins chains involved in the conversion remains, however, unknown. It has been hypothesized that the key controlling phenomenon is a selective amide hydration by water molecules (2). We previously investigated the role of hydration and concluded that water could either promote or inhibit transitions that are involved in silk spinning. Now, we wish to test the structural and dynamics events leading to conformational changes. The expected results will highlight how length and time scales play a role in the control of silk proteins storage and spinning.

Identifier
DOI https://doi.org/10.5286/ISIS.E.49918802
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/49918802
Provenance
Creator Dr Imke Greving; Dr Cedric Dicko; Dr Mark Telling; Professor Fritz Vollrath; Dr Christopher Holland; Dr Ann Terry
Publisher ISIS Neutron and Muon Source
Publication Year 2017
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2014-05-14T23:00:00Z
Temporal Coverage End 2014-05-19T23:00:00Z