In:
The Journal of Chemical Physics, AIP Publishing, Vol. 145, No. 3 ( 2016-07-21)
Abstract:
The homonuclear radio-frequency driven recoupling (RFDR) experiment is commonly used in solid-state NMR spectroscopy to gain insight into the structure of biological samples due to its ease of implementation, stability towards fluctuations/missetting of radio-frequency (rf) field strength, and in general low rf requirements. A theoretical operator-based Floquet description is presented to appreciate the effect of having a temporal displacement of the π-pulses in the RFDR experiment. From this description, we demonstrate improved transfer efficiency for the RFDR experiment by generating an adiabatic passage through the zero-quantum recoupling condition. We have compared the performances of RFDR and the improved sequence to mediate efficient 13CO to 13Cα polarization transfer for uniformly 13C,15N-labeled glycine and for the fibril forming peptide SNNFGAILSS (one-letter amino acid codes) uniformly 13C,15N-labeled at the FGAIL residues. Using numerically optimized sweeps, we get experimental gains of approximately 20% for glycine where numerical simulations predict an improvement of 25% relative to the standard implementation. For the fibril forming peptide, using the same sweep parameters as found for glycine, we have gains in the order of 10%–20% depending on the spectral regions of interest.
Type of Medium:
Online Resource
ISSN:
0021-9606
,
1089-7690
Language:
English
Publisher:
AIP Publishing
Publication Date:
2016
detail.hit.zdb_id:
3113-6
detail.hit.zdb_id:
1473050-9
