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dc.contributor.authorMadland, Eva
dc.contributor.authorKitaoku, Yoshihito
dc.contributor.authorSætrom, Gerd Inger
dc.contributor.authorLeth, Maria Louise
dc.contributor.authorEjby, Morten
dc.contributor.authorHachem, Maher Abou
dc.contributor.authorAachmann, Finn Lillelund
dc.date.accessioned2019-08-19T08:03:35Z
dc.date.available2019-08-19T08:03:35Z
dc.date.created2018-10-23T20:26:21Z
dc.date.issued2018
dc.identifier.citationBiomolecular NMR Assignments. 2018, .nb_NO
dc.identifier.issn1874-2718
dc.identifier.urihttp://hdl.handle.net/11250/2608903
dc.description.abstractThe N-terminal domain (residues 28–165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).nb_NO
dc.language.isoengnb_NO
dc.publisherSpringer Verlagnb_NO
dc.title1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalisnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber4nb_NO
dc.source.journalBiomolecular NMR Assignmentsnb_NO
dc.identifier.doi10.1007/s12104-018-9850-3
dc.identifier.cristin1622896
dc.relation.projectNorges forskningsråd: 226244nb_NO
dc.relation.projectNorges forskningsråd: 249797nb_NO
dc.description.localcodeThis is a post-peer-review, pre-copyedit version of an article published in [Biomolecular NMR Assignments] Locked until 22.9.2019 due to copyright restrictions. The final authenticated version is available online at: https://doi.org/10.1007/s12104-018-9850-3nb_NO
cristin.unitcode194,66,15,0
cristin.unitnameInstitutt for bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextpreprint
cristin.fulltextpostprint
cristin.qualitycode1


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