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dc.contributor.authorDobrovolska, Olena
dc.contributor.authorStrømland, Øyvind
dc.contributor.authorHandegård, Ørjan Sele
dc.contributor.authorJakubec, Martin
dc.contributor.authorGovasli Larsen, Morten Andreas
dc.contributor.authorSkjevik, Åge Aleksander
dc.contributor.authorFrøystein, Nils Åge
dc.contributor.authorTeigen, Knut
dc.contributor.authorHalskau, Øyvind
dc.date.accessioned2022-01-20T08:47:28Z
dc.date.available2022-01-20T08:47:28Z
dc.date.created2021-12-15T09:18:38Z
dc.date.issued2021
dc.identifier.issn1420-3049
dc.identifier.urihttps://hdl.handle.net/11250/2838403
dc.description.abstractThe driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using in silico analyses, NMR, conformational clustering, and Molecular Dynamics, we provide tentative insights into the conformations of bound and unbound A-Cage-C. The conformation of each state is dynamic and samples a large amount of overlapping conformational space. We identify one of the clusters as likely representing the binding conformation and conclude tentatively that the unfolding around the central W23 segment and its reorientation may be necessary for full intercalation at binding conditions (pH 4.5). We also see evidence for an overall elongation of A-Cage-C in the presence of model bilayers.en_US
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleInvestigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensemblesen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2021 by the authors.en_US
dc.source.articlenumber3607en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.doi10.3390/molecules26123607
dc.identifier.cristin1968628
dc.source.journalMoleculesen_US
dc.identifier.citationMolecules. 2021, 26 (12), 3607.en_US
dc.source.volume26en_US
dc.source.issue12en_US


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Navngivelse 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse 4.0 Internasjonal