ElectroProtein - Atomic-scale electrodynamics of protein-liquid interfaces

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Electrostatic and electrodynamic properties are fundamental physical properties that strongly influence biomolecular structure and functions. In particular, they regulate protein functions of fundamental biological importance, including enzymatic catalysis, protein-protein/ligand interactions, and transport of ions in protein channels. Importantly, they are strongly influenced by the properties of interfacial water layers near the protein surface or confined inside ion channels, which are different than in bulk water. Despite the huge impact, little is known about these properties due to the lack of experimental tools able to probe them on the molecular scale. Standard techniques such as nuclear magnetic resonance, dielectric-sensitive fluorescence microscopy, and impedance spectroscopy, lack the required spatial/temporal resolution or are influenced by several parameters that impede direct measurement. Furthermore, theorists struggle to predict these properties and need experimental data to benchmark their theories. A technique able to measure them on the molecular scale in their native liquid environment is much needed. Scanning Dielectric Microscopy (SDM) is a scanning probe microscopy technique recently introduced to probe these properties on the nanoscale. The challenge is now to push its resolution down to the molecular level and apply it to biological relevant molecules. In this project, the fellow will build on previous breakthroughs of the supervisor combining SDM and advanced 2D crystal technology to probe the electrodynamics of protein-liquid interface in liquid environment. The results of this action will allow gaining new fundamental knowledge and formulating better theories of proteins' functioning during complex biological processes.