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dc.contributor.authorHaselhorst, Thomasen_US
dc.contributor.authorK. Munster-Kuhnel, Anjaen_US
dc.contributor.authorOschlies, Melanieen_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.date.accessioned2017-04-24T09:19:41Z
dc.date.available2017-04-24T09:19:41Z
dc.date.issued2007en_US
dc.date.modified2009-09-01T06:00:51Z
dc.identifier.issn0006291Xen_US
dc.identifier.doi10.1016/j.bbrc.2007.05.204en_AU
dc.identifier.urihttp://hdl.handle.net/10072/18291
dc.description.abstractWe report an easy and direct application of 'Saturation Transfer Double Difference' (STDD) NMR spectroscopy to identify ligands that bind to a Sepharose-immobilised target protein. The model protein, cytidine 5'-monophosphate sialic acid (CMP-Sia) synthetase, was expressed as a Strep-Tag II fusion protein and immobilised on Strep-Tactinepharose. STD NMR experiments of the protein-enriched Sepharose matrix in the presence of a binding ligand (cytidine 5'-triphosphate, CTP) and a non-binding ligand (a/߭glucose) clearly show that CTP binds to the immobilised enzyme, whereas glucose has no affinity. This approach has three major advantages: (a) only low quantities of protein are required, (b) no specialised NMR technology or the application of additional data analysis by non-routine methods is required, and (c) easy multiple use of the immobilised protein is available.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevier Inc.en_US
dc.publisher.placeUnited Statesen_US
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description#descriptionen_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom866en_US
dc.relation.ispartofpageto870en_US
dc.relation.ispartofjournalBiochemical and Biophysical Research Communicationsen_US
dc.relation.ispartofvolume359en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchHISTORY AND ARCHAEOLOGYen_US
dc.subject.fieldofresearchcode210000en_US
dc.titleDirect detection of ligand binding to Sepharose-immobilised protein using saturation transfer double difference (STDD) NMR spectroscopyen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightCopyright 2007 Elsevier. Please refer to the journal's website for access to the definitive, published version.en_AU
gro.date.issued2007
gro.hasfulltextNo Full Text


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