Solvent-Mediated Proteome Stability: Elucidating Cold Unfolding Kinetics in Living Cells

Please discuss your project with a possible supervisor, Prof. Simon Ebbinghaus via email Simon.Ebbinghaus(at)rub.de before you fill out the application.

About the group and the topic

While classical thermodynamics has established the mechanisms of heat-induced protein denaturation, cold denaturation mechanisms remain elusive. Observing cold unfolding in proteins is crucial to understanding species adapted to low-temperature environments, yet remains extremely challenging as it typically occurs below 0^∘ "C" . In the crowded, non-ideal environment of a living cell, hydration dynamics and macromolecular crowding fundamentally alter protein stability curves, leading to structural instability at low temperatures. Precisely measuring these delicate thermodynamic transitions in real time requires sub-degree temperature control, high-resolution live-cell spectroscopy, and advanced structural probes. We invite pioneering researchers to overcome this complex analytical challenge: leverage state-of-the-art tools for live-cell analysis, such as Fast Relaxation Imaging Microscopy, to elucidate the thermodynamic forces driving cold-induced denaturation and set a new standard for research on functional proteins under extreme thermal conditions.

What they expect from students

From the applicants we would expect basic knowledge of biochemistry and spectroscopy. Experience in related fields is advantageous.

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Paper related to the topic