Differential Scanning Calorimetry of Protein–Lipid Interactions
dc.book.title | Lipid-Protein Interactions: Methods and Protocols | |
dc.contributor.author | Cañadas Benito, Olga | |
dc.contributor.author | Casals Carro, María Cristina | |
dc.contributor.editor | Kleinschmidt, Jörg H. | |
dc.date.accessioned | 2023-06-17T14:18:34Z | |
dc.date.available | 2023-06-17T14:18:34Z | |
dc.date.issued | 2019 | |
dc.description.abstract | Differential scanning calorimetry (DSC) is a highly sensitive nonperturbing technique used for studying the thermodynamic properties of thermally induced transitions. Since these properties might be affected by ligand binding, DSC is particularly useful for the characterization of protein interactions with biomimetic membranes. The advantages of this technique over other methods consist in the direct measurement of intrinsic thermal properties of the samples, requiring no chemical modifications or extrinsic probes. This chapter describes the basic theory of DSC and provides the reader with an understanding of the capabilities of DSC instrumentation and the type of information that can be achieved from DSC studies of lipid-protein interactions. In particular, the chapter provides a detailed analysis of DSC data to assess the effects of proteins on biomimetic membranes. | |
dc.description.department | Sección Deptal. de Bioquímica y Biología Molecular (Biológicas) | |
dc.description.faculty | Fac. de Ciencias Biológicas | |
dc.description.refereed | TRUE | |
dc.description.sponsorship | Ministerio de Economía y Competitividad (MINECO) | |
dc.description.sponsorship | Instituto de Salud Carlos III (ISCIII) | |
dc.description.status | pub | |
dc.eprint.id | https://eprints.ucm.es/id/eprint/60710 | |
dc.identifier.doi | 10.1007/978-1-4939-9512-7 | |
dc.identifier.isbn | 9781493995127 | |
dc.identifier.officialurl | https://link.springer.com/protocol/10.1007%2F978-1-4939-9512-7_5 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14352/14041 | |
dc.language.iso | eng | |
dc.page.final | 106 | |
dc.page.initial | 91 | |
dc.page.total | 682 | |
dc.publication.place | New York | |
dc.publisher | Humana Press | |
dc.relation.ispartofseries | Methods in Molecular Biology | |
dc.relation.projectID | (SAF2015-65307-R) | |
dc.relation.projectID | (CIBERES CB06/06/0002) | |
dc.rights.accessRights | restricted access | |
dc.subject.cdu | 577.1 | |
dc.subject.cdu | 577.2 | |
dc.subject.keyword | Differential scanning calorimetry | |
dc.subject.keyword | lipids | |
dc.subject.keyword | proteins | |
dc.subject.keyword | lipid–protein interaction | |
dc.subject.keyword | gel to liquid–crystalline phase transition | |
dc.subject.keyword | lamellar to inverted hexagonal phase transition | |
dc.subject.keyword | data analysis | |
dc.subject.ucm | Bioquímica (Biología) | |
dc.subject.unesco | 2302 Bioquímica | |
dc.title | Differential Scanning Calorimetry of Protein–Lipid Interactions | |
dc.type | book part | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | 25a89a2f-a381-4f15-9a6b-59430ee96a63 | |
relation.isAuthorOfPublication | d4e23d80-fa5c-4614-bd2d-2c391b596713 | |
relation.isAuthorOfPublication.latestForDiscovery | 25a89a2f-a381-4f15-9a6b-59430ee96a63 |
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