Intermolecular Packing in B. mori Silk Fibroin: Multinuclear NMR Study of the Model Peptide (Ala-Gly)15 Defines a Heterogeneous Antiparallel Antipolar Mode of Assembly in the Silk II Form

We have previously suggested that crystalline Bombyx mori silk in silk II form (the silk structure after spinning) is not a simple antiparallel β-sheet but is intrinsically heterogeneous. Using the peptide (AG)15, we have obtained the first fully assigned high resolution solid state 1H NMR spectrum....

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Veröffentlicht in:	Macromolecules 2015-01, Vol.48 (1), p.28-36
Hauptverfasser:	Asakura, Tetsuo, Ohata, Takuya, Kametani, Shunsuke, Okushita, Keiko, Yazawa, Koji, Nishiyama, Yusuke, Nishimura, Katsuyuki, Aoki, Akihiro, Suzuki, Furitsu, Kaji, Hironori, Ulrich, Anne S, Williamson, Mike P
Format:	Artikel
Sprache:	eng
Online-Zugang:	Volltext
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