Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein

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 se...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2022-10, Vol.16 (2), p.237-246
Main Authors: Wiedemann, Christoph, Obika, Kingsley Benjamin, Liebscher, Sandra, Jirschitzka, Jan, Ohlenschläger, Oliver, Bordusa, Frank
Format: Article
Language:English
Subjects:
Biochemistry
Biological and Medical Physics
Biophysics
NMR
Nuclear magnetic resonance
Physics
Physics and Astronomy
Polymer Sciences
Protein structure
Secondary structure
Structure-function relationships
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Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-022-10086-3