Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/116990
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dc.contributor.authorWiedemann, Christoph-
dc.contributor.authorObika, Kingsley Benjamin-
dc.contributor.authorLiebscher, Sandra-
dc.contributor.authorJirschitzka, Jan-
dc.contributor.authorOhlenschläger, Oliver-
dc.contributor.authorBordusa, Frank-
dc.date.accessioned2024-11-05T07:09:48Z-
dc.date.available2024-11-05T07:09:48Z-
dc.date.issued2022-
dc.identifier.urihttps://opendata.uni-halle.de//handle/1981185920/118950-
dc.identifier.urihttp://dx.doi.org/10.25673/116990-
dc.description.abstractThe 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.eng
dc.language.isoeng-
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/-
dc.subject.ddc572-
dc.titleBackbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 proteineng
dc.typeArticle-
local.versionTypepublishedVersion-
local.bibliographicCitation.journaltitleBiomolecular NMR assignments-
local.bibliographicCitation.volume16-
local.bibliographicCitation.publishernameSpringer Netherlands-
local.bibliographicCitation.publisherplaceDordrecht [u.a.]-
local.bibliographicCitation.doi10.1007/s12104-022-10086-3-
local.openaccesstrue-
dc.identifier.ppn1882413040-
cbs.publication.displayform2022-
local.bibliographicCitation.year2022-
cbs.sru.importDate2024-11-05T07:09:06Z-
local.bibliographicCitationEnthalten in Biomolecular NMR assignments - Dordrecht [u.a.] : Springer Netherlands, 2007-
local.accessrights.dnbfree-
Appears in Collections:Open Access Publikationen der MLU

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