Conformational study of 13C-enriched fibroin in the solid state, using the cross polarization nuclear magnetic resonance method.
Silk fibroin with the alanyl carboxyl carbon enriched with 13C was obtained by giving a diet containing 13C-enriched alanine to the larvae of Bombyx mori and Antheraea pernyi at the fifth instar. Sericin-free fibroin fibers were prepared from cocoons, and gut was made from the liquid silk in the gland. The final 13C content was about 13%. Cross polarization/magic angle sample spinning spectra at 25 MHz and 75 MHz were measured for each sample at different orientations. Spectra were simulated using the principal values and orientations of the shielding tensor in the alanine crystal. The results indicate that the beta-structure of the fibroin may be a little more flattened than the typical pleated sheet beta-structure.
D000818:Animals; D012831:Bombyx; D005349:Fibroins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation
D005349:Fibroins