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

Gregory P. Holland; Janelle E. Jenkins; Melinda S. Creager; Randolph V. Lewis; Jeffery L. Yarger

doi:10.1039/B812928B

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Chemical Communications

Issue 43, 2008

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

Gregory P. Holland , Janelle E. Jenkins , Melinda S. Creager , Randolph V. Lewis and Jeffery L. Yarger

Chem. Commun., 2008, 5568-5570

DOI: 10.1039/B812928B
Received 28 Jul 2008, Accepted 02 Sep 2008
First published on the web 29 Sep 2008

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Abstract
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Compounds
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Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and β-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in β-sheet structures is determined to be 82% ± 4% and 28% ± 5%, respectively.

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Consensus amino acid sequence of spider silk proteins,INADEQUATE pulse sequences and fit of the carbonyl resonance
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Gregory P. Holland
Janelle E. Jenkins
Melinda S. Creager
Randolph V. Lewis
Jeffery L. Yarger

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Chemical Communications

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

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