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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLEGER, Antoine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorAZOUZ, Mehdi
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.contributor.authorDOLE, Francois
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHOCQUELLET, Agnes
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCHAIGNEPAIN, Stephane
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCABANNE, Charlotte
dc.date.accessioned2021-07-09T07:45:19Z
dc.date.available2021-07-09T07:45:19Z
dc.date.issued2021
dc.identifier.issn1046-5928en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/106482
dc.description.abstractEnHsp12 is a small heat shock protein of Saccharomyces cerevisiae upregulated in response to various stresses. Non recombinant Hsp12 has been purified and characterized. Using circular dichroism (CD), Isothermal Titration Calorimetry (ITC) and Differential Scanning Calorimetry (DSC), it has been demonstrated that the native Hsp12 is monomeric and intrinsically disordered (IDP). Hsp12 gains in structure in the presence of specific lipids (PiP(2)). The helical form binds to liposomes models membrane with high affinity, leading to their rigidification. These results suggest that hydrophobic and ionic interactions are involved. Hsp12 is most likely a membrane chaperone expressed during stresses in Saccharomyces cerevisiae.
dc.language.isoENen_US
dc.subject.enSaccharomyces cerevisiae
dc.subject.enHeat shock protein
dc.subject.enIntrinsically disordered protein
dc.subject.enMembrane chaperone
dc.subject.enBiomembrane
dc.title.enPiP(2) favors an alpha-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.pep.2021.105830en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalProtein Expression and Purificationen_US
bordeaux.page7 p.en_US
bordeaux.volume181en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03282310
hal.version1
hal.date.transferred2021-07-09T07:45:23Z
hal.exporttrue
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