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Published on: June 29, 2021
Backbone Assignment of a 28.5 kDa Class A Extended Spectrum β-Lactamase by High-Field, Carbon-Detected Solid-State
Christopher G Williams1, Songlin Wang2,3, Alexander F Thome1
1Department of Chemistry, University of California, Riverside, Riverside, CA 92521, USA.
Abstract:
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 sidechain chemical shifts and catalytic mechanism.
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