التفاصيل البيبلوغرافية
| العنوان: |
Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2. |
| المؤلفون: |
Buchinger, Edith, Wiik, Siv Å., Kusnierczyk, Anna, Rabe, Renana, Aas, Per. A., Kavli, Bodil, Slupphaug, Geir, Aachmann, Finn L. |
| المصدر: |
Biomolecular NMR Assignments; Apr2018, Vol. 12 Issue 1, p15-22, 8p |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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