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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Autores principales: Wiedemann, Christoph, Obika, Kingsley Benjamin, Liebscher, Sandra, Jirschitzka, Jan, Ohlenschläger, Oliver, Bordusa, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510119/
https://www.ncbi.nlm.nih.gov/pubmed/35474152
http://dx.doi.org/10.1007/s12104-022-10086-3
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author Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschläger, Oliver
Bordusa, Frank
author_facet Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschläger, Oliver
Bordusa, Frank
author_sort Wiedemann, Christoph
collection PubMed
description 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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spelling pubmed-95101192022-09-27 Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein Wiedemann, Christoph Obika, Kingsley Benjamin Liebscher, Sandra Jirschitzka, Jan Ohlenschläger, Oliver Bordusa, Frank Biomol NMR Assign Article 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. Springer Netherlands 2022-04-26 2022 /pmc/articles/PMC9510119/ /pubmed/35474152 http://dx.doi.org/10.1007/s12104-022-10086-3 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visithttp://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/)
spellingShingle Article
Wiedemann, Christoph
Obika, Kingsley Benjamin
Liebscher, Sandra
Jirschitzka, Jan
Ohlenschläger, Oliver
Bordusa, Frank
Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title_full Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title_fullStr Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title_full_unstemmed Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title_short Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein
title_sort backbone and side chain resonance assignment of the intrinsically disordered human dbndd1 protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510119/
https://www.ncbi.nlm.nih.gov/pubmed/35474152
http://dx.doi.org/10.1007/s12104-022-10086-3
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