Issue 43, 2008
From the journal:

Chemical Communications

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

Gregory P. Holland,*a   Janelle E. Jenkins,a   Melinda S. Creager,b   Randolph V. Lewisb  and  Jeffery L. Yarger*a  

* Corresponding authors

a Department of Chemistry and Biochemistry, Magnetic Resonance Research Center, Arizona State University, Tempe, USA
E-mail: greg.holland@asu.edu, jyarger@gmail.com

b Department of Molecular Biology, University of Wyoming, Laramie, USA

Abstract

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.

Graphical abstract: 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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Article information

DOI
https://doi.org/10.1039/B812928B
Article type
Communication
Submitted
28 Jul 2008
Accepted
02 Sep 2008
First published
29 Sep 2008

Chem. Commun., 2008, 5568-5570

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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

G. P. Holland, J. E. Jenkins, M. S. Creager, R. V. Lewis and J. L. Yarger, Chem. Commun., 2008, 5568 DOI: 10.1039/B812928B

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