<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Nimerovsky E</submitter><funding>Deutsche Forschungsgemeinschaft</funding><funding>Max-Planck-Gesellschaft</funding><pagination>2763-2771</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10598565</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>3(10)</volume><pubmed_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 differe</pubmed_abstract><journal>JACS Au</journal><pubmed_title>Simplified Preservation of Equivalent Pathways Spectroscopy.</pubmed_title><pmcid>PMC10598565</pmcid><funding_grant_id>AN1316</funding_grant_id><pubmed_authors>Andreas LB</pubmed_authors><pubmed_authors>Varkey AC</pubmed_authors><pubmed_authors>Becker S</pubmed_authors><pubmed_authors>Kim M</pubmed_authors><pubmed_authors>Nimerovsky E</pubmed_authors></additional><is_claimable>false</is_claimable><name>Simplified Preservation of Equivalent Pathways Spectroscopy.</name><description>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 differe</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Oct</publication><modification>2026-05-29T07:34:18.238Z</modification><creation>2026-05-16T03:07:34.458Z</creation></dates><accession>S-EPMC10598565</accession><cross_references><pubmed>37885577</pubmed><doi>10.1021/jacsau.3c00312</doi></cross_references></HashMap>