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

Biomol NMR Assign

Charles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.

Published: October 2022

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510119PMC
http://dx.doi.org/10.1007/s12104-022-10086-3DOI Listing

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