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<p><sup>13</sup>C and <sup>15</sup>N backbone chemical shift assignments are reported for the 28.5&#xa0;kDa protein Toho-1 β-lactamase, a Class A extended spectrum β-lactamase. A very high level of assignment completeness (97% of the backbone) is enabled by the combined sensitivity and resolution gains of ultrahigh-field NMR spectroscopy (1.1&#xa0;GHz), improved probe technology, and optimized pulse sequences. The assigned chemical shifts agree well with our previous solution-state NMR assignments, indicating that the secondary structure is conserved in the solid state. These assignments provide a foundation for future investigations of side-chain chemical shifts and catalytic mechanism.</p>

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Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR

  • 期刊论文

  • 发表日期：

    2025年7月27日

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  • Christopher G. Williams,
  • Songlin Wang,
  • Alexander F. Thome,
  • Owen A. Warmuth,
  • Varun Sakhrani,
  • Leighton Coates,
  • Chad M. Rienstra,
  • Leonard J. Mueller

摘要

13C and 15N backbone chemical shift assignments are reported for the 28.5 kDa protein Toho-1 β-lactamase, a Class A extended spectrum β-lactamase. A very high level of assignment completeness (97% of the backbone) is enabled by the combined sensitivity and resolution gains of ultrahigh-field NMR spectroscopy (1.1 GHz), improved probe technology, and optimized pulse sequences. The assigned chemical shifts agree well with our previous solution-state NMR assignments, indicating that the secondary structure is conserved in the solid state. These assignments provide a foundation for future investigations of side-chain chemical shifts and catalytic mechanism.