Speaker
Cécilia Siri
(EPFL)
Description
Recent study has reignited interest in the physiological implications of protein interaction with intracellular small molecules, particularly their weak non-specific interaction believed to influence many protein properties. Here, we take ubiquitin as a model to examine in depth by NMR its interaction with proline, an amino acid present prevalently in cellular environment. Our findings show that proline interacts weakly with ubiquitin but at specific hotspots consistent with a patchy model. The results are used to explain the enhancement of colloidal stability of ubiquitin by proline.
Author
Cécilia Siri
(EPFL)
Co-author
Francesco Stellacci
(EPFL)
