Hierarchical mobility in silk proteins - implication for storage and spinning
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. The dynamics of the water and protein chains involved in the conversion remains, however, unknown. Building upon our newly developed deuterium exchange method; and, the performance of the IN16B spectrometer (faster, good dynamic range allowing access to both the internal and center-of-mass diffusion of proteins in solution); we wish to determine the global and internal dynamics leading to conformational changes in silk proteins in aqueous solution (D2O and H2O). The expected results will determine how hierarchical mobility plays a role in the control of silk proteins storage, aggregation, and spinning. The data analysis will build upon recently published frameworks to separate the contributions from the solvent water, internal, and global motions [M.Grimaldo et al., EPJ Web conf.83, 02005 (2015) and references therein].
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DICKO Cedric; GREENHALGH Alex; GREVING Imke; HOLLAND Chris; SEYDEL Tilo; TERRY Ann and VOLLRATH Fritz. (2017). Hierarchical mobility in silk proteins - implication for storage and spinning. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-803
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