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Journal Article

Simplified Preservation of Equivalent Pathways Spectroscopy

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Nimerovsky,  Evgeny
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Varkey,  Abel Cherian
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Kim,  Myeongkyu
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Becker,  Stefan
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Andreas,  Loren B.
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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nimerovsky-et-al-2023
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Citation

Nimerovsky, E., Varkey, A. C., Kim, M., Becker, S., & Andreas, L. B. (2023). Simplified Preservation of Equivalent Pathways Spectroscopy. JACS Au, 3(10), 2763-2771. doi:10.1021/jacsau.3c00312.


Cite as: https://hdl.handle.net/21.11116/0000-000D-BC2A-1
Abstract
Inspired by the recently proposed transverse mixing optimal control pulses (TROP) approach for improving signal in multidimensional magic-angle spinning (MAS) NMR experiments, we present simplified preservation of equivalent pathways spectroscopy (SPEPS). It transfers both transverse components of magnetization that occur during indirect evolutions, theoretically enabling a √2 improvement in sensitivity for each such dimension. We compare SPEPS transfer with TROP and cross-polarization (CP) using membrane protein and fibril samples at MAS of 55 and 100 kHz. In three-dimensional (3D) (H)CANH spectra, SPEPS outperformed TROP and CP by factors of on average 1.16 and 1.69, respectively, for the membrane protein, but only a marginal improvement of 1.09 was observed for the fibril. These differences are discussed, making note of the longer transfer time used for CP, 14 ms, as compared with 2.9 and 3.6 ms for SPEPS and TROP, respectively. Using SPEPS for two transfers in the 3D (H)CANCO experiment resulted in an even larger benefit in signal intensity, with an average improvement of 1.82 as compared with CP. This results in multifold time savings, in particular considering the weaker peaks that are observed to benefit the most from SPEPS.