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dc.contributor.authorBaines, Cameron
dc.contributor.otherOldham, Neil
dc.contributor.otherSargeant, Jacob
dc.contributor.otherFage, Christopher
dc.contributor.otherPugh, Hannah
dc.contributor.otherAlkhalaf, Lona
dc.contributor.otherChallis, Gregory
dc.description.abstractRaw native-MS and IM-MS data supporting publication in JASMS. Abstract: Collision induced unfolding (CIU) of protein ions, monitored by ion mobility-mass spectrometry (IM-MS), can be used to assess the stability of their compact gas-phase fold, and hence provide structural information. The bacterial elongation factor EF-Tu, a key protein for protein translation in prokaryotes, and hence a promising antibiotic target, has been studied by CIU. The major [M+12H]12+ ion of EF-Tu unfolded in collision with Ar atoms between 40 and 50 V, corresponding to an Elab energy of 480-500 eV. Binding of the cofactor analogue GDPNP and the antibiotic enacyloxin IIa stabilized the compact fold of EF-Tu, although dissociation of the latter from the complex diminished its stabilizing effect at higher collision energiesen_UK
dc.publisherThe University of Nottinghamen_UK
dc.subject.lcshMass spectrometryen_UK
dc.subject.lcshIon mobility spectroscopyen_UK
dc.subject.lcshProteins -- Structureen_UK
dc.titleNative ESI-MS and Collision Induced Unfolding (CIU) of the Complex between Bacterial Elongation Factor-Tu and the Antibiotic Enacyloxin IIaen_UK
dc.subject.freeMass Spectrometry IM-MS Native-MS EF-Tu CID CIUen_UK
dc.subject.jacsPhysical sciences::Chemistry::Organic chemistry::Biomolecular chemistryen_UK
dc.subject.lcQ Science::QD Chemistry::QD241 Organic chemistry::QD415 Biochemistryen_UK
uon.divisionUniversity of Nottingham, UK Campus::Faculty of Science::School of Chemistryen_UK
uon.funder.controlledBiotechnology & biological Sciences Research Councilen_UK
uon.datatypeMass Spectrometry Data Filesen_UK
uon.collectionmethodWaters Synapt G1 HDMS High Definition Mass Spectrometeren_UK

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