Universität zu Köln

Wiedemann, Christoph, Obika, Kingsley Benjamin, Liebscher, Sandra ORCID: 0000-0001-9582-8473, Jirschitzka, Jan ORCID: 0000-0003-1007-4700, Ohlenschlaeger, Oliver and Bordusa, Frank (2022). Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein. Biomol. NMR Assign., 16 (2). S. 237 - 247. DORDRECHT: SPRINGER. ISSN 1874-270X

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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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Wiedemann, Christoph UNSPECIFIED UNSPECIFIED UNSPECIFIED Obika, Kingsley Benjamin UNSPECIFIED UNSPECIFIED UNSPECIFIED Liebscher, Sandra UNSPECIFIED orcid.org/0000-0001-9582-8473 UNSPECIFIED Jirschitzka, Jan UNSPECIFIED orcid.org/0000-0003-1007-4700 UNSPECIFIED Ohlenschlaeger, Oliver UNSPECIFIED UNSPECIFIED UNSPECIFIED Bordusa, Frank UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-678599
DOI:	10.1007/s12104-022-10086-3
Journal or Publication Title:	Biomol. NMR Assign.
Volume:	16
Number:	2
Page Range:	S. 237 - 247
Date:	2022
Publisher:	SPRINGER
Place of Publication:	DORDRECHT
ISSN:	1874-270X
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language NMR-SPECTROSCOPY; LARGER PROTEINS; CHEMICAL-SHIFTS; C-13; SENSITIVITY; DYSBINDIN; AMIDE; N-15; PREDICTION; SPECTRA Multiple languages Biophysics; Spectroscopy Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/67859