Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein.
Backbone and side chain nuclear magnetic resonance assignments
Chemical shifts
Dysbindin domain-containing protein 1 (DBNDD1)
Dystrobrevin-binding protein
Intrinsically disordered protein (IDP)
Solution NMR
Solution state nuclear magnetic resonance
Journal
Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371
Informations de publication
Date de publication:
10 2022
10 2022
Historique:
received:
11
02
2022
accepted:
05
04
2022
pubmed:
28
4
2022
medline:
28
9
2022
entrez:
27
4
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35474152
doi: 10.1007/s12104-022-10086-3
pii: 10.1007/s12104-022-10086-3
pmc: PMC9510119
doi:
Substances chimiques
Dysbindin
0
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
237-246Informations de copyright
© 2022. The Author(s).
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