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-quantu
Dipolar double-quantum filtered rotational-echo double resonance
โ Scribed by Shigeru Matsuoka; Jacob Schaefer
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 315 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0749-1581
- DOI
- 10.1002/mrc.2076
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โฆ Synopsis
The homonuclear dipolar coupling of a directly bonded 13 C-13 C pair has been used to create a dipolar double-quantum filter (D-DQF) to remove the natural-abundance 13 C background in 13 Cf 2 Hg rotationalecho double-resonance (REDOR) experiments. The most efficient version of this experiment has the D-DQF excitation and reconversion preceding the REDOR evolution period. Calculated and observed 13 Cf 2 Hg D-DQF-REDOR dephasings were in agreement for a test sample of mixed recrystallized labeled alanines.
๐ SIMILAR VOLUMES
## REDOR is a magic-angle spinning experiment for measuring internuclear distances between heteronuclear spin pairs. The basic principles of the REDOR technique are presented. The experimental requirements necessary for quantitative REDOR measurements are also provided.
A carbon-13 magic angle spinning double-quantum filtered dipolar shift correlation NMR experiment which can be used to establish through-space connectivities in solids is analyzed. The main advantage of the double-quantum filtered approach is the removal of intensity arising from natural abundance b
We present a new technique for double-quantum excitation in magic-angle-spinning solid-state NMR. The method involves (i) preparation of nonequilibrium longitudinal magnetization; (ii) mechanical excitation of zero-quantum coherence by spinning the sample at rotational resonance, and (iii) phase-coh