Universität zu Köln

Wiedemann, Christoph, Obika, Kingsley Benjamin, Liebscher, Sandra ORCID: 0000-0001-9582-8473, Jirschitzka, Jan ORCID: 0000-0003-1007-4700, Ohlenschlager, Oliver and Bordusa, Frank (2021). Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered. Biomol. NMR Assign., 15 (2). S. 441 - 449. DORDRECHT: SPRINGER. ISSN 1874-270X

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Abstract

Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these unknown proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the H-1, C-13, N-15 backbone and near-complete side-chain chemical shift assignments indicate that it is 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 Ohlenschlager, Oliver UNSPECIFIED UNSPECIFIED UNSPECIFIED Bordusa, Frank UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-584769
DOI:	10.1007/s12104-021-10043-6
Journal or Publication Title:	Biomol. NMR Assign.
Volume:	15
Number:	2
Page Range:	S. 441 - 449
Date:	2021
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; SECONDARY STRUCTURE; C-13; SENSITIVITY; RESONANCES; AMIDE; N-15; PREDICTION; SPECTRA Multiple languages Biophysics; Spectroscopy Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/58476