期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 40, 页码 12402-12407出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1511308112
关键词
thermodynamics; protein stability; crowding; in vivo; NMR
资金
- Swedish Research Council
- Swedish Foundation for Strategic Research [MDB1-0030]
- Hjarnfonden
- Knut and Alice Wallenberg Foundation
- Bertil Hallsten Foundation
- Magnus Bergwall Foundation
- European Council [261863]
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.
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