Abstract
The apo-form of the 24.4 kDa AA9 family lytic polysaccharide monooxygenase TaLPMO9A from Thermoascus aurantiacus has been isotopically labeled and recombinantly expressed in Pichia pastoris. In this paper, we report the 1H, 13C, and 15N chemical shift assignments, as well as an analysis of the secondary structure of the protein based on the secondary chemical shifts.
Original language | English |
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Pages (from-to) | 357-361 |
Number of pages | 5 |
Journal | Biomolecular NMR Assignments |
Volume | 12 |
Issue number | 2 |
DOIs | |
Publication status | Published - Oct 2018 |
Keywords
- Apoenzymes/chemistry
- Cellulose/metabolism
- Mixed Function Oxygenases/chemistry
- Nuclear Magnetic Resonance, Biomolecular
- Thermoascus/enzymology