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dc.contributor.authorAachmann, Finn Lillelund
dc.contributor.authorSørlie, Morten
dc.contributor.authorSkjåk-Bræk, Gudmund
dc.contributor.authorEijsink, Vincent
dc.contributor.authorVaaje-Kolstad, Gustav
dc.date.accessioned2017-09-05T09:24:10Z
dc.date.available2017-09-05T09:24:10Z
dc.date.created2012-11-12T23:01:14Z
dc.date.issued2012
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America. 2012, 109 (46), 18779-18784.nb_NO
dc.identifier.issn0027-8424
dc.identifier.urihttp://hdl.handle.net/11250/2453160
dc.language.isoengnb_NO
dc.titleNMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactionsnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber18779-18784nb_NO
dc.source.volume109nb_NO
dc.source.journalProceedings of the National Academy of Sciences of the United States of Americanb_NO
dc.source.issue46nb_NO
dc.identifier.doi10.1073/pnas.1208822109
dc.identifier.cristin961610
dc.relation.projectNorges forskningsråd: 214138nb_NO
dc.relation.projectNorges forskningsråd: 209335nb_NO
dc.relation.projectNorges forskningsråd: 196885nb_NO
dc.relation.projectNorges forskningsråd: 182695nb_NO
dc.relation.projectNorges forskningsråd: 186946nb_NO
cristin.unitcode192,12,0,0
cristin.unitnameKjemi, bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode2


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