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Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C

dc.contributor.authorCourtade, Gaston
dc.contributor.authorForsberg, Zarah
dc.contributor.authorVaaje-Kolstad, Gustav
dc.contributor.authorEijsink, Vincentius Gerardus Henricus
dc.contributor.authorAachmann, Finn Lillelund
dc.date.accessioned2017-10-30T11:34:06Z
dc.date.available2017-10-30T11:34:06Z
dc.date.created2017-08-21T09:25:38Z
dc.date.issued2017
dc.identifier.citationBiomolecular NMR Assignments. 2017, 11 (2), 257-264.nb_NO
dc.identifier.issn1874-2718
dc.identifier.urihttp://hdl.handle.net/11250/2462833
dc.description.abstractThe apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and recombinantly expressed in Escherichia coli. In this paper, we report the 1H, 13C, and 15N chemical shift assignments of each individual domain as well as an ensemble of the assignment for the full-length protein, including its approximately 30-amino acid long linker.nb_NO
dc.language.isoengnb_NO
dc.publisherSpringer Verlagnb_NO
dc.titleChemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10Cnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber257-264nb_NO
dc.source.volume11nb_NO
dc.source.journalBiomolecular NMR Assignmentsnb_NO
dc.source.issue2nb_NO
dc.identifier.doi10.1007/s12104-017-9759-2
dc.identifier.cristin1487532
dc.relation.projectNorges forskningsråd: 226244nb_NO
dc.relation.projectNorges forskningsråd: 221576nb_NO
dc.description.localcode© Springer Verlag. The final publication is available at https://link.springer.com/article/10.1007%2Fs12104-017-9759-2. This is the authors' accepted and refereed manuscript to the article. Locked until 18.8.2018 due to copyright restrictions.nb_NO
cristin.unitcode194,66,15,0
cristin.unitnameInstitutt for bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode1


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