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dc.contributor.author
Danielsson, Jens
dc.contributor.author
Mu, Xin
dc.contributor.author
Lang, Lisa
dc.contributor.author
Wang, Huabing
dc.contributor.author
Binolfi, Andrés
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dc.contributor.author
Theillet, François Xavier
dc.contributor.author
Bekei, Beata
dc.contributor.author
Logan, Derek T.
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Selenko, Philipp
dc.contributor.author
Wennerström, Håkan
dc.contributor.author
Oliveberg, Mikael
dc.date.available
2018-07-18T17:55:31Z
dc.date.issued
2015-10
dc.identifier.citation
Danielsson, 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.identifier.issn
0027-8424
dc.identifier.uri
http://hdl.handle.net/11336/52589
dc.description.abstract
Although 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.format
application/pdf
dc.language.iso
eng
dc.publisher
National Academy of Sciences
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Crowding
dc.subject
In Vivo
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Nmr
dc.subject
Protein Stability
dc.subject
Thermodynamics
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Thermodynamics of protein destabilization in live cells
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-07-17T13:55:28Z
dc.journal.volume
112
dc.journal.number
40
dc.journal.pagination
12402-12407
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Washington
dc.description.fil
Fil: Danielsson, Jens. Stockholms Universitet; Suecia
dc.description.fil
Fil: Mu, Xin. Stockholms Universitet; Suecia
dc.description.fil
Fil: Lang, Lisa. Stockholms Universitet; Suecia
dc.description.fil
Fil: Wang, Huabing. Stockholms Universitet; Suecia
dc.description.fil
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Leibniz Institute of Molecular Pharmacology; Alemania
dc.description.fil
Fil: Theillet, François Xavier. Leibniz Institute of Molecular Pharmacology; Alemania
dc.description.fil
Fil: Bekei, Beata. Leibniz Institute of Molecular Pharmacology; Alemania
dc.description.fil
Fil: Logan, Derek T.. Lund University; Suecia
dc.description.fil
Fil: Selenko, Philipp. Leibniz Institute of Molecular Pharmacology; Alemania
dc.description.fil
Fil: Wennerström, Håkan. Lund University; Suecia
dc.description.fil
Fil: Oliveberg, Mikael. Stockholms Universitet; Suecia
dc.journal.title
Proceedings of the National Academy of Sciences of The United States of America
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1073/pnas.1511308112
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/112/40/12402
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