Conformational constraints in solid-state NMR of uniformly labeled polypeptides from double single-quantum-filtered rotational echo double resonance
✍ Scribed by Nathan A. Oyler; Robert Tycko
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 458 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0749-1581
- DOI
- 10.1002/mrc.2110
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✦ Synopsis
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 15 N, 13 C labeling of consecutive pairs of amino acids or of longer segments. The technique, called double single-quantumfiltered rotational echo double resonance (DSQ-REDOR), uses frequency-selective REDOR to prepare DSQ coherences involving directly bonded backbone 13 CO and 15 NH sites, to dephase these coherences under longer-range 15 NH-13 CO dipole-dipole couplings in a conformationally dependent manner, and to convert the remaining DSQ coherences to detectable transverse 13 C-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 Ab 11 -25 . Published in 2007 by John Wiley & Sons, Ltd.