FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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Thermodynamics of protein destabilization in live cells
Danielsson(*), J., Mu(*), X., Lang(*), L., Wang(*), H., Binolfi, A., Theillet, F. X., Bekei, B., Logan(*), D. T., Selenko, P., Wennerstrom(*), H.; Oliveberg(*), M.
Proc Natl Acad Sci U S A, 112:12402-12407

Tags: In-Cell NMR (Selenko)

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 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.

Copper binding to the N-terminally acetylated, naturally occurring form of alpha-synuclein induces local helical folding
Miotto(*), M. C., Valiente-Gabioud(*), A. A., Rossetti(*), G., Zweckstetter(*), M., Carloni(*), P., Selenko, P., Griesinger(*), C., Binolfi, A.; Fernandez(*), C. O.
J Am Chem Soc, 137:6444-6447

Tags: In-Cell NMR (Selenko)

Abstract: Growing evidence supports a link between brain copper homeostasis, the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally acetylated (AcAS). Here we used NMR spectroscopy to structurally characterize the interaction between Cu(I) and AcAS. We found that the formation of an AcAS-Cu(I) complex at the N-terminal region stabilizes local conformations with alpha-helical secondary structure and restricted motility. Our work provides new evidence into the metallo-biology of PD and opens new lines of research as the formation of AcAS-Cu(I) complex might impact on AcAS membrane binding and aggregation.

Real-time NMR monitoring of biological activities in complex physiological environments
Smith(*), M. J., Marshall(*), C. B., Theillet, F. X., Binolfi, A., Selenko, P.; Ikura(*), M.
Curr Opin Struct Biol, 32:39-47

Tags: In-Cell NMR (Selenko)

Abstract: Biological reactions occur in a highly organized spatiotemporal context and with kinetics that are modulated by multiple environmental factors. To integrate these variables in our experimental investigations of 'native' biological activities, we require quantitative tools for time-resolved in situ analyses in physiologically relevant settings. Here, we outline the use of high-resolution NMR spectroscopy to directly observe biological reactions in complex environments and in real-time. Specifically, we discuss how real-time NMR (RT-NMR) methods have delineated insights into metabolic processes, post-translational protein modifications, activities of cellular GTPases and their regulators, as well as of protein folding events.

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)

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