Quantifying the fraction of glycine and alanine in β-sheet and helical conformations in spider dragline silk using solid-state NMR
Literature Information
Gregory P. Holland, Janelle E. Jenkins, Melinda S. Creager, Randolph V. Lewis, Jeffery L. Yarger
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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![9H-Fluoren-9-ylmethyl {15-[(2,5-dioxo-1-pyrrolidinyl)oxy]-15-oxo-3,6,9,12-tetraoxapentadec-1-yl}carbamate structure 9H-Fluoren-9-ylmethyl {15-[(2,5-dioxo-1-pyrrolidinyl)oxy]-15-oxo-3,6,9,12-tetraoxapentadec-1-yl}carbamate structure](https://static.chemtradehub.com/structs/131/1314378-14-7-4316.webp)

