Change search
ReferencesLink to record
Permanent link

Direct link
Thermodynamics of protein destabilization in live cells
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
Number of Authors: 11
2015 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 112, no 40, 12402-12407 p.Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
2015. Vol. 112, no 40, 12402-12407 p.
Keyword [en]
thermodynamics, protein stability, crowding, in vivo, NMR
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-123537DOI: 10.1073/pnas.1511308112ISI: 000363125400053OAI: oai:DiVA.org:su-123537DiVA: diva2:874590
Available from: 2015-11-27 Created: 2015-11-27 Last updated: 2015-11-27Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Danielsson, JensMu, XinLang, LisaWang, HuabingOliveberg, Mikael
By organisation
Department of Biochemistry and Biophysics
In the same journal
Proceedings of the National Academy of Sciences of the United States of America
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 12 hits
ReferencesLink to record
Permanent link

Direct link