Abstract
Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major ampullate spidroin 2 (MaSp2).
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Elastin / chemistry
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Fibroins / chemistry*
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Magnetic Resonance Spectroscopy
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Protein Structure, Secondary
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Spiders
Substances
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spidroin 2
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Elastin
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Fibroins