Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | Burgos, Martha Ines | - |
| dc.creator | Dassie, Sergio Alberto | - |
| dc.creator | Villarreal, Marcos Ariel | - |
| dc.creator | Fidelio, Gerardo Daniel | - |
| dc.date | 2018-10-09T16:35:56Z | - |
| dc.date | 2018-10-09T16:35:56Z | - |
| dc.date | 2012-02 | - |
| dc.date | 2018-09-18T16:16:34Z | - |
| dc.date.accessioned | 2019-04-29T15:44:15Z | - |
| dc.date.available | 2019-04-29T15:44:15Z | - |
| dc.date.issued | 2018-10-09T16:35:56Z | - |
| dc.date.issued | 2018-10-09T16:35:56Z | - |
| dc.date.issued | 2012-02 | - |
| dc.date.issued | 2018-09-18T16:16:34Z | - |
| dc.identifier | Burgos, Martha Ines; Dassie, Sergio Alberto; Villarreal, Marcos Ariel; Fidelio, Gerardo Daniel; Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1824; 2; 2-2012; 383-391 | - |
| dc.identifier | 1570-9639 | - |
| dc.identifier | http://hdl.handle.net/11336/61967 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/300711 | - |
| dc.description | The energetics of protein homo-oligomerization was analyzed in detail with the application of a general thermodynamic model. We have studied the thermodynamic aspects of protein-protein interaction employing β-lactoglobulin A from bovine milk at pH = 6.7 where the protein is mainly in its dimeric form. We performed differential calorimetric scans at different total protein concentration and the resulting thermograms were analyzed with the thermodynamic model for oligomeric proteins previously developed. The thermodynamic model employed, allowed the prediction of the sign of the enthalpy of dimerization, the analysis of complex calorimetric profiles without transitions baselines subtraction and the obtainment of the thermodynamic parameters from the unfolding and the association processes and the compared with association parameters obtained with Isothermal Titration Calorimetry performed at different temperatures. The dissociation and unfolding reactions were also monitored by Fourier-transform infrared spectroscopy and the results indicated that the dimer of β-lactoglobulin (N 2) reversibly dissociates into monomeric units (N) which are structurally distinguishable by changes in their infrared absorbance spectra upon heating. Hence, it is proposed that β-lactoglobulin follows the conformational path induced by temperature:N 2 ⇌ 2N ⇌ 2D. The general model was validated with these results indicating that it can be employed in the study of the thermodynamics of other homo-oligomeric protein systems. © 2011 Elsevier B.V. All rights reserved. | - |
| dc.description | Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina | - |
| dc.description | Fil: Dassie, Sergio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina | - |
| dc.description | Fil: Villarreal, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina | - |
| dc.description | Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Elsevier Science | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.bbapap.2011.11.005 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S1570963911003128 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/61967 | - |
| dc.subject | Β-LACTOGLOBULIN | - |
| dc.subject | DIFFERENTIAL SCANNING CALORIMETRY | - |
| dc.subject | FOURIER-TRANSFORMED INFRARED SPECTROSCOPY | - |
| dc.subject | OLIGOMERIC PROTEIN | - |
| dc.subject | PROTEIN STABILITY | - |
| dc.subject | THERMODYNAMIC MODEL | - |
| dc.subject | Otras Ciencias Biológicas | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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