Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.creatorDanielsson, Jens-
dc.creatorMu, Xin-
dc.creatorLang, Lisa-
dc.creatorWang, Huabing-
dc.creatorBinolfi, Andrés-
dc.creatorTheillet, François Xavier-
dc.creatorBekei, Beata-
dc.creatorLogan, Derek T.-
dc.creatorSelenko, Philipp-
dc.creatorWennerström, Håkan-
dc.creatorOliveberg, Mikael-
dc.date2018-07-18T17:55:31Z-
dc.date2018-07-18T17:55:31Z-
dc.date2015-10-
dc.date2018-07-17T13:55:28Z-
dc.date.accessioned2019-04-29T15:43:32Z-
dc.date.available2019-04-29T15:43:32Z-
dc.date.issued2018-07-18T17:55:31Z-
dc.date.issued2018-07-18T17:55:31Z-
dc.date.issued2015-10-
dc.date.issued2018-07-17T13:55:28Z-
dc.identifierDanielsson, Jens; Mu, Xin; Lang, Lisa; Wang, Huabing; Binolfi, Andrés; et al.; Thermodynamics of protein destabilization in live cells; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 112; 40; 10-2015; 12402-12407-
dc.identifier0027-8424-
dc.identifierhttp://hdl.handle.net/11336/52589-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/300398-
dc.descriptionAlthough protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a ß-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro crowding effects, we find that the cells destabilize the protein at 37°C but with a conspicuous twist While the melting temperature goes down the cold unfolding moves into the physiological regime, coupled to an augmented heat-capacity change. The effect seems induced by transient, sequence-specific, interactions with the cellular components, acting preferentially on the unfolded ensemble. This points to a model where the in vivo influence on protein behavior is case specific, determined by the individual protein's interplay with the functionally optimized "interaction landscape" of the cellular interior.-
dc.descriptionFil: Danielsson, Jens. Stockholms Universitet; Suecia-
dc.descriptionFil: Mu, Xin. Stockholms Universitet; Suecia-
dc.descriptionFil: Lang, Lisa. Stockholms Universitet; Suecia-
dc.descriptionFil: Wang, Huabing. Stockholms Universitet; Suecia-
dc.descriptionFil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Leibniz Institute of Molecular Pharmacology; Alemania-
dc.descriptionFil: Theillet, François Xavier. Leibniz Institute of Molecular Pharmacology; Alemania-
dc.descriptionFil: Bekei, Beata. Leibniz Institute of Molecular Pharmacology; Alemania-
dc.descriptionFil: Logan, Derek T.. Lund University; Suecia-
dc.descriptionFil: Selenko, Philipp. Leibniz Institute of Molecular Pharmacology; Alemania-
dc.descriptionFil: Wennerström, Håkan. Lund University; Suecia-
dc.descriptionFil: Oliveberg, Mikael. Stockholms Universitet; Suecia-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherNational Academy of Sciences-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1073/pnas.1511308112-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/112/40/12402-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectCROWDING-
dc.subjectIN VIVO-
dc.subjectNMR-
dc.subjectPROTEIN STABILITY-
dc.subjectTHERMODYNAMICS-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleThermodynamics of protein destabilization in live cells-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.