Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5407903 | Journal of Magnetic Resonance | 2006 | 15 Pages |
Abstract
Silk from the wild silkworm Samia cynthia ricini with a molecular mass of about 300 kDa consists of alternating repeats of nano-crystalline poly-(Ala) and non-crystalline glycine-rich domains. The backbone torsion angles between pairs of these two amino acids is determined by DOQSY solid-state NMR spectroscopy: the alanine-rich domains are predominantly in a β-sheet conformation, whereas the glycine-rich domains are found to be partially in an extended β-sheet conformation and partially in an approximately 31-helical conformation. In the cast film from liquid silk significantly different secondary structures were found: the alanine-rich domains are α-helical conformation, whereas the results for glycine-labelled sample are explained by a random-coil state. A detailed error analysis of the technique is presented.
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Authors
Jacco D. van Beek, Beat H. Meier,