Artículo
Thermodynamics of protein destabilization in live cells
Danielsson, Jens; Mu, Xin; Lang, Lisa; Wang, Huabing; Binolfi, Andrés
; Theillet, François Xavier; Bekei, Beata; Logan, Derek T.; Selenko, Philipp; Wennerström, Håkan; Oliveberg, Mikael
![Icon](/themes/CONICETDigital/images/conicet.png)
Fecha de publicación:
10/2015
Editorial:
National Academy of Sciences
Revista:
Proceedings of the National Academy of Sciences of The United States of America
ISSN:
0027-8424
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
Crowding
,
In Vivo
,
Nmr
,
Protein Stability
,
Thermodynamics
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Articulos(CCT - ROSARIO)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - ROSARIO
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - ROSARIO
Citación
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
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