Browsing Publikasjoner fra CRIStin - NTNU by Journals "Biomolecular NMR Assignments"
Now showing items 1-7 of 7
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1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis
(Journal article; Peer reviewed, 2018)The N-terminal domain (residues 28–165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and ... -
1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10Afrom Jonesia denitrificans
(Peer reviewed; Journal article, 2020)The lytic polysaccharide monooxygenase JdLPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated JdLPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to ... -
1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis
(Journal article; Peer reviewed, 2015)The chitin-active 19.2 kDa lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis has been isotopically labeled and recombinantly expressed. In this paper, we report the 1H, 13C, 15N resonance assignment ... -
Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2
(Journal article; Peer reviewed, 2017)Human uracil N-glycosylase isoform 2—UNG2 consists of an N-terminal intrinsically disordered regulatory domain (UNG2 residues 1–92, 9.3 kDa) and a C-terminal structured catalytic domain (UNG2 residues 93–313, 25.1 kDa). ... -
Backbone and side-chain 1H, 13C, and 15N chemical shift assignments for the apo-form of the lytic polysaccharide monooxygenase NcLPMO9C
(Journal article; Peer reviewed, 2016)The apo-form of the 23.3 kDa catalytic domain of the AA9 family lytic polysaccharide monooxygenase NcLPMO9C from Neurospora crassa has been isotopically labeled and recombinantly expressed in Pichia pastoris. In this paper, ... -
Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C
(Journal article; Peer reviewed, 2017)The apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and ... -
Resonance assignments for the apo-form of the cellulose-active lytic polysaccharide monooxygenase TaLPMO9A
(Journal article; Peer reviewed, 2018)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 ...