Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Angelani, Carla Romina | - |
| dc.creator | Curto, Lucrecia María | - |
| dc.creator | Cabanas, Inés S | - |
| dc.creator | Caramelo, Julio Javier | - |
| dc.creator | Uversky, Vladimir N | - |
| dc.creator | Delfino, Jose Maria | - |
| dc.date | 2016-11-29T21:18:19Z | - |
| dc.date | 2016-11-29T21:18:19Z | - |
| dc.date | 2014-09 | - |
| dc.date | 2016-11-29T12:42:31Z | - |
| dc.date.accessioned | 2019-04-29T15:32:04Z | - |
| dc.date.available | 2019-04-29T15:32:04Z | - |
| dc.date.issued | 2016-11-29T21:18:19Z | - |
| dc.date.issued | 2016-11-29T21:18:19Z | - |
| dc.date.issued | 2014-09 | - |
| dc.date.issued | 2016-11-29T12:42:31Z | - |
| dc.identifier | Angelani, Carla Romina; Curto, Lucrecia María; Cabanas, Inés S; Caramelo, Julio Javier; Uversky, Vladimir N; et al.; Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1844; 9; 9-2014; 1599-1607 | - |
| dc.identifier | 1570-9639 | - |
| dc.identifier | http://hdl.handle.net/11336/8480 | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/295934 | - |
| dc.description | Δ78Δ is a second generation functional all-β sheet variant of IFABP (intestinal fatty acid binding protein) corresponding to the fragment 29-106 of the parent protein. This protein and its predecessor, Δ98Δ (segment 29-126 of IFABP), were initially uncovered by controlled proteolysis. Remarkably, although IFABP and Δ98Δ are monomers in solution, Δ78Δ adopts a stable dimeric structure. With the aim of identifying key structural features that modulate the aggregation of β-proteins, we evaluate here the structure and aggregation propensity of Δ78Δ. The 2,2,2-trifluoroethanol (TFE) induced aggregation of this protein shows a primary nucleation-elongation mechanism, characterized by the stabilization of a dimeric nucleus. Its rate of production from the co-solvent induced aggregation prone state governs the kinetics of polymerization. In this context, the value of Δ78Δ lies in the fact that - being a stable dimeric species - it reduces an otherwise bimolecular reaction to a unimolecular one. Interestingly, even though Δ78Δ and IFABP display similar conformational stability, the abrogated form of IFABP shows an enhanced aggregation rate, revealing the ancillary role played on this process by the free energy of the native proteins. Δ78Δ share with IFABP and Δ98Δ a common putative aggregation-prone central peptide. Differences in the exposure/accessibility of this segment dictated by the environment around this region might underlie the observed variations in the speed of aggregation. Lessons learnt from this natural dimeric protein might shed light on the early conformational events leading to β-conversion from barrels to amyloid aggregates. | - |
| dc.description | Fil: Angelani, Carla Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina | - |
| dc.description | Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina | - |
| dc.description | Fil: Cabanas, Inés S. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina | - |
| dc.description | Fil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina | - |
| dc.description | Fil: Uversky, Vladimir N. Russian Academy of Sciences. Institute for Biological Instrumentation; Rusia. University of South Florida. Department of Molecular Medicine; Estados Unidos | - |
| dc.description | Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Elsevier Science | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963914001514 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbapap.2014.06.002 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | FABP | - |
| dc.subject | amiloide | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species | - |
| 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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