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| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | Paz, Sergio Alexis | - |
| dc.creator | Vanden-Eijnden, Eric | - |
| dc.creator | Abrams, Cameron F. | - |
| dc.date | 2018-10-12T17:15:04Z | - |
| dc.date | 2018-10-12T17:15:04Z | - |
| dc.date | 2017-08-30 | - |
| dc.date | 2018-09-10T15:47:00Z | - |
| dc.date.accessioned | 2019-04-29T15:37:56Z | - |
| dc.date.available | 2019-04-29T15:37:56Z | - |
| dc.date.issued | 2017-08-30 | - |
| dc.identifier | Paz, Sergio Alexis; Vanden-Eijnden, Eric; Abrams, Cameron F.; Polymorphism at 129 dictates metastable conformations of the human prion protein N-terminal β-sheet; Royal Society of Chemistry; Chemical Science; 8; 2; 30-8-2017; 1225-1232 | - |
| dc.identifier | 2041-6520 | - |
| dc.identifier | http://hdl.handle.net/11336/62313 | - |
| dc.identifier | 2041-6539 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298121 | - |
| dc.description | We study the thermodynamic stability of the native state of the human prion protein using a new free-energy method, replica-exchange on-the-fly parameterization. This method is designed to overcome hidden-variable sampling limitations to yield nearly error-free free-energy profiles along a conformational coordinate. We confirm that all four (M129V, D178N) polymorphs have a ground-state conformation with three intact β-sheet hydrogen bonds. Additionally, they are observed to have distinct metastabilities determined by the side-chain at position 129. We rationalize these findings with reference to the prion “strain” hypothesis, which links the variety of transmissible spongiform encephalopathy phenotypes to conformationally distinct infectious prion forms and classifies distinct phenotypes of sporadic Creutzfeldt-Jakob disease based solely on the 129 polymorphism. Because such metastable structures are not easily observed in structural experiments, our approach could potentially provide new insights into the conformational origins of prion diseases and other pathologies arising from protein misfolding and aggregation. | - |
| dc.description | Fil: Paz, Sergio Alexis. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Drexel University; Estados Unidos | - |
| dc.description | Fil: Vanden-Eijnden, Eric. University of New York; Estados Unidos | - |
| dc.description | Fil: Abrams, Cameron F.. Drexel University; Estados Unidos | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Royal Society of Chemistry | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/Content/ArticleLanding/2017/SC/C6SC03275C | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1039/C6SC03275C | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| 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/11336/62313 | - |
| dc.subject | FREE ENERGY | - |
| dc.subject | PRION PROTEIN | - |
| dc.subject | REPLICA EXCHANGE | - |
| dc.subject | OTFP | - |
| dc.subject | Otras Ciencias Químicas | - |
| dc.subject | Ciencias Químicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Polymorphism at 129 dictates metastable conformations of the human prion protein N-terminal β-sheet | - |
| 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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