Quantifying the fraction of glycine and alanine in beta-sheet and helical conformations in spider dragline silk using solid-state NMR

Quantifying the fraction of glycine and alanine in beta-sheet and helical conformations in spider dragline silk using solid-state NMR

Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and beta-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in beta-sheet structures is determined to be 82% +/- 4%...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2008-01 (43), p.5568-5570
Hauptverfasser: Holland, Gregory P, Jenkins, Janelle E, Creager, Melinda S, Lewis, Randolph V, Yarger, Jeffery L
Format: Artikel
Sprache:eng
Schlagworte:
Alanine - chemistry
Animals
Carbon Isotopes
Glycine - chemistry
Magnetic Resonance Spectroscopy - methods
Magnetic Resonance Spectroscopy - standards
Protein Structure, Secondary
Reference Standards
Silk - chemistry
Spiders
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Zusammenfassung:Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and beta-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in beta-sheet structures is determined to be 82% +/- 4% and 28% +/- 5%, respectively.
ISSN:1359-7345
1364-548X
DOI:10.1039/b812928b