Cargando…

Simplified Preservation of Equivalent Pathways Spectroscopy

[Image: see text] 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 transver...

Descripción completa

Detalles Bibliográficos
Autores principales: Nimerovsky, Evgeny, Varkey, Abel Cherian, Kim, Myeongkyu, Becker, Stefan, Andreas, Loren B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10598565/
https://www.ncbi.nlm.nih.gov/pubmed/37885577
http://dx.doi.org/10.1021/jacsau.3c00312
_version_ 1785125582110982144
author Nimerovsky, Evgeny
Varkey, Abel Cherian
Kim, Myeongkyu
Becker, Stefan
Andreas, Loren B.
author_facet Nimerovsky, Evgeny
Varkey, Abel Cherian
Kim, Myeongkyu
Becker, Stefan
Andreas, Loren B.
author_sort Nimerovsky, Evgeny
collection PubMed
description [Image: see text] 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.
format Online
Article
Text
id pubmed-10598565
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-105985652023-10-26 Simplified Preservation of Equivalent Pathways Spectroscopy Nimerovsky, Evgeny Varkey, Abel Cherian Kim, Myeongkyu Becker, Stefan Andreas, Loren B. JACS Au [Image: see text] 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. American Chemical Society 2023-10-11 /pmc/articles/PMC10598565/ /pubmed/37885577 http://dx.doi.org/10.1021/jacsau.3c00312 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Nimerovsky, Evgeny
Varkey, Abel Cherian
Kim, Myeongkyu
Becker, Stefan
Andreas, Loren B.
Simplified Preservation of Equivalent Pathways Spectroscopy
title Simplified Preservation of Equivalent Pathways Spectroscopy
title_full Simplified Preservation of Equivalent Pathways Spectroscopy
title_fullStr Simplified Preservation of Equivalent Pathways Spectroscopy
title_full_unstemmed Simplified Preservation of Equivalent Pathways Spectroscopy
title_short Simplified Preservation of Equivalent Pathways Spectroscopy
title_sort simplified preservation of equivalent pathways spectroscopy
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10598565/
https://www.ncbi.nlm.nih.gov/pubmed/37885577
http://dx.doi.org/10.1021/jacsau.3c00312
work_keys_str_mv AT nimerovskyevgeny simplifiedpreservationofequivalentpathwaysspectroscopy
AT varkeyabelcherian simplifiedpreservationofequivalentpathwaysspectroscopy
AT kimmyeongkyu simplifiedpreservationofequivalentpathwaysspectroscopy
AT beckerstefan simplifiedpreservationofequivalentpathwaysspectroscopy
AT andreaslorenb simplifiedpreservationofequivalentpathwaysspectroscopy