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Thermodynamics of protein destabilization in live cells
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Vise andre og tillknytning
Rekke forfattare: 112015 (engelsk)Inngår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 112, nr 40, s. 12402-12407Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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 beta-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 degrees 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.

sted, utgiver, år, opplag, sider
2015. Vol. 112, nr 40, s. 12402-12407
Emneord [en]
thermodynamics, protein stability, crowding, in vivo, NMR
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-123537DOI: 10.1073/pnas.1511308112ISI: 000363125400053OAI: oai:DiVA.org:su-123537DiVA, id: diva2:874590
Tilgjengelig fra: 2015-11-27 Laget: 2015-11-27 Sist oppdatert: 2017-12-01bibliografisk kontrollert

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