Preprints
https://doi.org/10.5194/mr-2024-9
https://doi.org/10.5194/mr-2024-9
05 Jun 2024
 | 05 Jun 2024
Status: a revised version of this preprint was accepted for the journal MR.

PRESERVE: adding variable flip-angle excitation to TROSY NMR spectroscopy

Bernhard Brutscher

Abstract. We introduce the PRESERVE pulse sequence element, allowing variable flip-angle adjustment in 2D 1H-15N and 1H-13C TROSY-type correlation experiments. PRESERVE-TROSY exploits a remarkable array of up to nine orthogonal polarization-coherence transfer pathways, showcasing the remarkable potential of spin manipulations achievable through the design and optimization of NMR pulse sequences.

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Bernhard Brutscher

Status: final response (author comments only)

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2024-9', Anonymous Referee #1, 07 Jun 2024
    • AC2: 'Reply on RC1', Bernhard Brutscher, 17 Jun 2024
  • RC2: 'Comment on mr-2024-9', Eriks Kupce, 11 Jun 2024
    • AC3: 'Reply on RC2', Bernhard Brutscher, 17 Jun 2024
  • RC3: 'Comment on mr-2024-9', Teodor Parella, 13 Jun 2024
    • AC4: 'Reply on RC3', Bernhard Brutscher, 17 Jun 2024
  • AC1: 'Comment on mr-2024-9', Bernhard Brutscher, 17 Jun 2024
Bernhard Brutscher
Bernhard Brutscher

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Short summary
We introduce the PRESERVE pulse sequence element, allowing variable flip-angle adjustment in 2D 1H-15N and 1H-13C TROSY-type correlation experiments. PRESERVE-TROSY exploits a remarkable array of up to nine orthogonal polarization-coherence transfer pathways, showcasing the remarkable potential of spin manipulations achievable through the design and optimization of NMR pulse sequences.