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<p>Methyl groups are essential probes for characterising interactions and dynamics in large proteins. HN-based triple-resonance NMR experiments are often too insensitive for methyl assignments, making a NOESY-based approach an efficient strategy. Linking geminal methyl groups in leucine and valine residues is a crucial step in such NOESY-based methyl resonance assignment strategies. This link can be established unambiguously with the 3D-HMBC-HMQC experiment, introduced for large U-[<sup>12</sup>C, <sup>2</sup>H] LV-[<sup>13</sup>CH<sub>3</sub>]<sub>2</sub>-labelled proteins. Here, we introduce the SOFAST variant of the 3D-HMBC-HMQC experiment which provides spectra with fewer artefacts arising from the water signal and a mean increase in signal-to-noise ratio per unit time of 16% compared to the original experiment with an optimised recovery delay.</p>

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The SOFAST-HMBC-HMQC experiment for pairing geminal methyl groups in valine and leucine side-chains

  • 期刊论文

  • 发表日期：

    2025年4月7日

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  • Ana Paula Aguilar Alva,
  • Lucas Siemons,
  • Ulric B. le Paige,
  • Coline Wiame,
  • Florence Cordier,
  • Nicolas Wolff,
  • Guillaume Bouvignies,
  • Philippe Pelupessy,
  • Fabien Ferrage

摘要

Methyl groups are essential probes for characterising interactions and dynamics in large proteins. HN-based triple-resonance NMR experiments are often too insensitive for methyl assignments, making a NOESY-based approach an efficient strategy. Linking geminal methyl groups in leucine and valine residues is a crucial step in such NOESY-based methyl resonance assignment strategies. This link can be established unambiguously with the 3D-HMBC-HMQC experiment, introduced for large U-[12C, 2H] LV-[13CH3]2-labelled proteins. Here, we introduce the SOFAST variant of the 3D-HMBC-HMQC experiment which provides spectra with fewer artefacts arising from the water signal and a mean increase in signal-to-noise ratio per unit time of 16% compared to the original experiment with an optimised recovery delay.