Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization
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In this work, we show how the water flip-back approach that is widely employed in solution-state NMR can be adapted to proton-detected MAS solid-state NMR of highly deuterated proteins. The scheme allows to enhance the sensitivity of the experiment by decreasing the recovery time of the proton longitudinal magnetization. The method relies on polarization transfer from non-saturated water to the protein during the inter-scan delay.
KeywordsMagic angle spinning (MAS) solid-state NMR Perdeuteration Sensitivity enchancement Protein water interaction
We thank Brigitta Angerstein for expert technical assistance. This work was supported by the Max Planck Society, the Leibniz-Gemeinschaft, and the DFG (Emmy Noether Fellowship to A.L). A.L. and S.X. acknowledge funding from the CRC803 (DFG).
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