期刊
JOURNAL OF CHEMICAL PHYSICS
卷 145, 期 3, 页码 -出版社
AMER INST PHYSICS
DOI: 10.1063/1.4958318
关键词
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资金
- Danish Council for Independent Research [DFF-4090-00223]
- Villum Foundation [VKR023122]
- Swiss National Science Foundation [200020_124611, 200020_134681]
- ETH Zurich [ETH-10 15-1]
- Danish National Research Foundation [DNRF 0059]
- Carlsbergfondet
- Aarhus University
- Danish Ministry of Higher Education and Science [AU-2010-612-181]
- Villum Fonden [00007271] Funding Source: researchfish
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 p-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 (CO)-C-13 to C-13(alpha) polarization transfer for uniformly C-13, N-15-labeled glycine and for the fibril forming peptide SNNFGAILSS (one-letter amino acid codes) uniformly C-13, N-15-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. Published by AIP Publishing.
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