PiP(2) favors an alpha-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae
| dc.rights.license | open | en_US |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | LEGER, Antoine | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | AZOUZ, Mehdi | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | LECOMTE, Sophie | |
| dc.contributor.author | DOLE, Francois | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | HOCQUELLET, Agnes | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | CHAIGNEPAIN, Stephane | |
| hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
| dc.contributor.author | CABANNE, Charlotte | |
| dc.date.accessioned | 2021-07-09T07:45:19Z | |
| dc.date.available | 2021-07-09T07:45:19Z | |
| dc.date.issued | 2021 | |
| dc.identifier.issn | 1046-5928 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/106482 | |
| dc.description.abstractEn | Hsp12 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.iso | EN | en_US |
| dc.subject.en | Saccharomyces cerevisiae | |
| dc.subject.en | Heat shock protein | |
| dc.subject.en | Intrinsically disordered protein | |
| dc.subject.en | Membrane chaperone | |
| dc.subject.en | Biomembrane | |
| dc.title.en | PiP(2) favors an alpha-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae | |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1016/j.pep.2021.105830 | en_US |
| dc.subject.hal | Chimie/Matériaux | en_US |
| bordeaux.journal | Protein Expression and Purification | en_US |
| bordeaux.page | 7 p. | en_US |
| bordeaux.volume | 181 | en_US |
| bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | en_US |
| bordeaux.institution | Université de Bordeaux | en_US |
| bordeaux.institution | Bordeaux INP | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| hal.identifier | hal-03282310 | |
| hal.version | 1 | |
| hal.date.transferred | 2021-07-09T07:45:23Z | |
| hal.export | true | |
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