Efficient low-power heteronuclear decoupling in 13C high-resolution solid-state NMR under fast magic angle spinning
β Scribed by Mrignayani Kotecha; Nalinda P. Wickramasinghe; Yoshitaka Ishii
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 504 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0749-1581
- DOI
- 10.1002/mrc.2151
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β¦ Synopsis
The use of a low-power two-pulse phase modulation (TPPM) sequence is proposed for efficient 1 H radio frequency (rf) decoupling in high-resolution 13 C solid-state NMR (SSNMR) under fast MAS conditions. Decoupling efficiency for different low-power decoupling sequences such as continuous-wave (cw), TPPM, XiX, and p-pulse (PIPS) train decoupling has been investigated at a spinning speed of 40 kHz for 13 C CPMAS spectra of uniformly 13 C-and 15 N-labeled L-alanine. It was found that the TPPM decoupling sequence, which was originally designed for high-power decoupling, provides the best decoupling efficiency at low power among all the low-power decoupling sequences examined here. Optimum performance of the low-power TPPM sequence was found to be obtained at a decoupling field intensity (! 1 ) of βΌ! R /4 with a pulse flip angle of βΌp and a phase alternation between Β±f.f = βΌ20Β°/, where ! R /2p is the spinning speed. The sensitivity obtained for 13 CO 2 -, 13 CH, and 13 CH 3 in L-alanine under low-power TPPM at ! 1 /2p of 10 kHz was only 5-15% less than that under high-power TPPM at ! 1 /2p of 200 kHz, despite the fact that only 0.25% of the rf power was required in low-power TPPM. Analysis of the 13 CH 2 signals for uniformly 13 C-and 15 N-labeled L-isoleucine under various low-power decoupling sequences also confirmed superior performance of the low-power TPPM sequence, although the intensity obtained by low-power TPPM was 61% of that obtained by high-power TPPM. 13 C CPMAS spectra of 13 C-labeled ubiquitin micro crystals obtained by low-power TPPM demonstrates that the low-power TPPM sequence is a practical option that provides excellent resolution and sensitivity in 13 C SSNMR for hydrated proteins.
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