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Default 3D 15N/15N/1H Chemical Shift Correlation Experiment Utilizing an RFDR-based 1H/1H Mixing Period at 100 kHz MAS

3D 15N/15N/1H Chemical Shift Correlation Experiment Utilizing an RFDR-based 1H/1H Mixing Period at 100 kHz MAS

Publication date: Available online 19 April 2014
Source:Journal of Magnetic Resonance

Author(s): Yusuke Nishiyama , Michal Malon , Yuji Ishii , Ayyalusamy Ramamoorthy

Homonuclear correlation NMR experiments are commonly used in the high-resolution structural studies of proteins. While 13C/13C chemical shift correlation experiments utilizing dipolar recoupling techniques are fully utilized under MAS, correlation of the chemical shifts of 15N nuclei in proteins has been a challenge. Previous studies have shown that the negligible 15N-15N dipolar coupling in peptides or proteins necessitates the use of a very long mixing time (typically several seconds) for effective spin diffusion to occur and considerably slows down a 15N/15N correlation experiment. In this study, we show that the use of mixing proton magnetization, instead of 15N, via the recoupled 1H-1H dipolar couplings enable faster 15N/15N correlation. In addition, the use of proton-detection under ultrafast MAS overcomes the sensitivity loss due to multiple magnetization transfer (between 1H and 15N nuclei) steps. In fact, less than 300 nL (~1.1 micromole quantity) sample is sufficient to acquire the 3D spectrum within 5 hours. Our results also demonstrate that a 3D 15N/15N/1H experiment can render higher resolution spectra that will be useful in the structural studies of proteins at ultrafast MAS frequencies. 3D 15N/15N/1H and 2D radio frequency-driven dipolar recoupling (RFDR)-based 1H/1H experimental results obtained from a powder sample of N-acetyla-L-15N-valyl-L-15N-leucine at 70 and 100 kHz MAS frequencies are presented.
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