This article is a US Government work and is in the public domain in the USA
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Research Article
Conformational constraints in solid-state NMR of uniformly labeled polypeptides from double single-quantum-filtered rotational echo double resonance†
Article first published online: 21 DEC 2007
DOI: 10.1002/mrc.2110
This article is a US Government work and is in the public domain in the USA. Published in 2007 by John Wiley & Sons, Ltd.
Issue
1097-458Xa/asset/cover.gif?v=1&s=d5f2b3f6d127fcc37c26f1dbdb0c8887da653c0f "Magnetic Resonance in Chemistry")
Magnetic Resonance in Chemistry
Special Issue: New techniques in solid-state NMR
Volume 45, Issue S1, pages S101–S106, December 2007
Additional Information
How to Cite
Oyler, N. A. and Tycko, R. (2007), Conformational constraints in solid-state NMR of uniformly labeled polypeptides from double single-quantum-filtered rotational echo double resonance. Magn. Reson. Chem., 45: S101–S106. doi: 10.1002/mrc.2110
- †
Publication History
- Issue published online: 21 DEC 2007
- Article first published online: 21 DEC 2007
- Manuscript Accepted: 17 SEP 2007
- Manuscript Revised: 12 SEP 2007
- Manuscript Received: 15 JUN 2007
Funded by
- This work was supported by the Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases
- Intramural AIDS Targeted Antiviral Program of the National Institutes of Health
Keywords:
- NMR;
- 13C;
- 15N;
- protein structure;
- magic-angle spinning;
- amyloid;
- dipolar recoupling
Abstract
A solid-state nuclear magnetic resonance (NMR) technique is described for obtaining constraints on the backbone conformation of a protein or peptide that is prepared with uniform 15N,13C labeling of consecutive pairs of amino acids or of longer segments. The technique, called double single-quantum-filtered rotational echo double resonance (DSQ-REDOR), uses frequency-selective REDOR to prepare DSQ coherences involving directly bonded backbone 13CO and 15NH sites, to dephase these coherences under longer-range 15NH![[BOND]](http://onlinelibrarystatic.wiley.com/undisplayable_characters/00f8ff.gif)
13CO dipole-dipole couplings in a conformationally dependent manner, and to convert the remaining DSQ coherences to detectable transverse 13C-spin polarization. The efficacy of DSQ-REDOR is demonstrated in experiments on two isotopically labeled samples, the helical peptide MB(i + 4)EK and the amyloid-forming peptide Aβ11–25. Published in 2007 John Wiley & Sons, Ltd.