Abstract
Band-selective pulses are frequently used in multi-dimensional NMR in solution, but have been used relatively less often in solid-state NMR applications because of the complications imposed by magic-angle spinning. In this work, we examine the frequency profiles and the refocusing efficiency of several commonly employed selective general rotation π pulses through experiments and numerical simulations. We demonstrate that highly efficient refocusing of transverse magnetization can be achieved, with experiments that agree well with numerical simulations. We also show that the rotational echo is shifted by a half rotor period if a selective pulse is applied over an integer number of rotor periods. Appropriately synchronizing indirect evolution periods with selective pulses ensures proper phasing of cross peaks in 2D spectra. The improved performance of selective pulses in multi-dimensional protein spectroscopy is demonstrated on the 56-residue β1 immunoglobulin binding domain of protein G (GB1).
Original language | English (US) |
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Pages (from-to) | 206-216 |
Number of pages | 11 |
Journal | Journal of Magnetic Resonance |
Volume | 179 |
Issue number | 2 |
DOIs | |
State | Published - Apr 2006 |
Keywords
- Protein
- Rotational echo
- Scalar coupling
- Selective pulses
- Solid-state NMR spectroscopy
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Nuclear and High Energy Physics
- Condensed Matter Physics