Structural stability of silk proteins in D2O by SANS
The formation of silk fibres in both spiders and silkworms is characterized by a conversion of short range ordered structures in solution into long range ordered beta-sheet rich structures in the final fibre. For silk we hypothesise that local flexibility of the protein chain will mediate silk protein storage/beta-sheet aggregation. To understand the mechanism we propose to study how concentration affects the local flexibility of silk fibroin both in its reactive (native) state and in a un-natural reconstituted silk fibroin. The results will have an impact on how we control silk storage and stability as well as for other hydrogen bonding polymers and proteins
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DICKO Cedric; GREVING Imke; GRILLO Isabelle; HOLLAND Chris; Mark T F Telling; TERRY Ann and VOLLRATH Fritz. (2014). Structural stability of silk proteins in D2O by SANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-562
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