Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2

Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2

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). Here, we report the backbone 1 H, 13 C, and 15 N chemical shift assignment as w...

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Veröffentlicht in:Biomolecular NMR assignments 2018-04, Vol.12 (1), p.15-22
Hauptverfasser: Buchinger, Edith, Wiik, Siv Å., Kusnierczyk, Anna, Rabe, Renana, Aas, Per. A., Kavli, Bodil, Slupphaug, Geir, Aachmann, Finn L.
Format: Artikel
Sprache:eng
Schlagworte:
Biochemistry
Biological and Medical Physics
Biophysics
Physics
Physics and Astronomy
Polymer Sciences
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Zusammenfassung: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). Here, we report the backbone 1 H, 13 C, and 15 N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-017-9772-5