Refined Crystal Structure of Samia cynthia ricini Silk Fibroin Revealed by Solid-State NMR Investigations.
Related Articles Refined Crystal Structure of Samia cynthia ricini Silk Fibroin Revealed by Solid-State NMR Investigations.
Biomacromolecules. 2017 Jun 12;18(6):1965-1974
Authors: Asakura T, Nishimura A, Kametani S, Kawanishi S, Aoki A, Suzuki F, Kaji H, Naito A
Abstract
Samia cynthia ricini is one of the wild silkworms and its silk fibroin (SF) consists of alternatively repeating poly-l-alanine (PLA) sequences as crystalline domain and glycine-rich sequences as noncrystalline domain; the structure is similar to those of spider silk and other wild silkworm silks. In this paper, we proposed a new staggered model for the packing arrangement of the PLA sequence through the use of the Cambridge Serial Total Energy Package program and a comparison of the observed and calculated chemical shifts of the PLA sequence with the Gauge Including Projector Augmented Wave method. The new model was supported by the interatomic distance information from the cross peaks of Ala C? dipolar-assisted rotational resonance (DARR) spectrum of the PLA sequences in S. c. ricini SF fiber. In addition, three 13C NMR peaks observed in the ?-sheet region were assigned to the carbons with different environments in the same model, but not assigned to different ?-sheet structures.
PMID: 28505425 [PubMed - indexed for MEDLINE]
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