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Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2.
Buchinger, Edith; Wiik, Siv Å; Kusnierczyk, Anna; Rabe, Renana; Aas, Per A; Kavli, Bodil; Slupphaug, Geir; Aachmann, Finn L.
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  • Buchinger E; NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Wiik SÅ; NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Kusnierczyk A; Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, 0317, Oslo, Norway.
  • Rabe R; Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Aas PA; Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Kavli B; Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Slupphaug G; Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
  • Aachmann FL; Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
Biomol NMR Assign ; 12(1): 15-22, 2018 04.
Article em En | MEDLINE | ID: mdl-28879561
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 1H, 13C, and 15N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ressonância Magnética Nuclear Biomolecular / DNA Glicosilases Idioma: En Ano de publicação: 2018 Tipo de documento: Article
Texto completo
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XML
PubMed Links
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ressonância Magnética Nuclear Biomolecular / DNA Glicosilases Idioma: En Ano de publicação: 2018 Tipo de documento: Article