Solid-state nuclear magnetic resonance (NMR) spectroscopy reveals distinctive protein dynamics in closely related spider silks

Structurally closely related spider silks, namely, major ampullate silk (MaS) reeled at 0.5 and 10 cm/s, minor ampullate silk (MiS), and cocoon silk have been investigated by solid-state nuclear magnetic resonance (NMR). These silks exhibit different mechanical properties that are not well explained with current structural data. NMR spectra confirm that the secondary structures of these silks are similar, but that differing relaxation dynamics exist at the alanine, glycine, and glutamine residue level. MaS reeled rapidly is made of more mobile proteins in both the beta-sheet and amorphous regions, suggesting that reeling speed alters molecular rearrangement during spinning, with the chain packing being less organized in the fastpull fiber. Alanine and glycine relaxation dynamics increases as MaS < MiS < cocoon silk, showing that the whole fiber displays distinctive protein dynamics, chain packing, and intermolecular interactions. Besides molecular orientation, silk extensibility is related to a more mobile structural organization.