Please use this identifier to cite or link to this item:
http://dx.doi.org/10.25673/116990| Title: | Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein |
| Author(s): | Wiedemann, Christoph Obika, Kingsley Benjamin Liebscher, Sandra Jirschitzka, Jan Ohlenschläger, Oliver Bordusa, Frank |
| Issue Date: | 2022 |
| Type: | Article |
| Language: | English |
| Abstract: | 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. |
| URI: | https://opendata.uni-halle.de//handle/1981185920/118950 http://dx.doi.org/10.25673/116990 |
| Open Access: |  Open access publication |
| License: |  (CC BY 4.0) Creative Commons Attribution 4.0 |
| Journal Title: | Biomolecular NMR assignments |
| Publisher: | Springer Netherlands |
| Publisher Place: | Dordrecht [u.a.] |
| Volume: | 16 |
| Original Publication: | 10.1007/s12104-022-10086-3 |
| Appears in Collections: | Open Access Publikationen der MLU |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| s12104-022-10086-3.pdf | 3.36 MB | Adobe PDF |  View/Open |