The specific structures, Silk I and Lamella, observed in the sequence model peptides, (Ala-Gly)(n) of Bombyx mori silk fibroin, could be determined by several C-13 solid state NMR techniques coupled with C-13 selective labeling of the peptides. The former is the silk fibroin structure before spinning that is a key structure in order to clarify the mechanism of formation of the silk fiber with exceptional strength and toughness from the aqueous solution in silkworm. The latter is a unique structure related with Silk II as referred to the silk fibroin structure after spinning and useful in molecular design the biomaterials with silk. The C-13 solid state NMR coupled with C-13/N-15 stable isotope labeling is very useful to clarify these specific structures appeared in the fibrous protein and therefore the process of the determination is described in detail.
CITATION STYLE
Asakura, T., Suzuki, Y., & Nakazawa, Y. (2014). The Silk I and Lamella Structures of (Ala-Gly)15 as the Model of Bombyx mori Silk Fibroin Studied with Solid State NMR (pp. 49–68). https://doi.org/10.1007/978-94-007-7119-2_3
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