无规卷曲人 DBNDD1 蛋白的骨架和侧链共振赋值。
Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein.
机构信息
Charles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.
Faculty of Chemistry and Earth Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, Biostructural Interactions, Friedrich Schiller University Jena, Humboldtstraße 10, 07743, Jena, Germany.
出版信息
Biomol NMR Assign. 2022 Oct;16(2):237-246. doi: 10.1007/s12104-022-10086-3. Epub 2022 Apr 26.
The dysbindin domain-containing protein 1 (DBNDD1) is a conserved protein among higher eukaryotes whose structure and function are poorly investigated so far. Here, we present the backbone and side chain nuclear magnetic resonance assignments for the human DBNDD1 protein. Our chemical-shift based secondary structure analysis reveals the human DBNDD1 as an intrinsically disordered protein.
该蛋白包含 dysbindin 结构域蛋白 1（DBNDD1）是一种在高等真核生物中高度保守的蛋白，但它的结构和功能至今仍未得到充分研究。在这里，我们给出了人 DBNDD1 蛋白的骨架和侧链核磁共振波谱归属。基于化学位移的二级结构分析表明，人 DBNDD1 是一种固有无序蛋白。
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