LMP Seminar: Spin’s eye view on protein motions in dilute and condensed phases

Cellular functions are mediated by translational and reorientational motions of biomolecules at various length- and timescales. In a large class of eukaryotic proteins called intrinsically disordered proteins (IDPs), protein dynamics occur at multiple length- and timescales that are not accessible to a single experimental technique. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique enabling detection and quantification of protein motions at atomistic resolution. In my talk, I will present a highly integrative approach, combining NMR spin relaxation at low and high magnetic fields with molecular dynamic (MD) simulation and other biophysical techniques, to address multiscale dynamics in IDPs. Following this approach in the case of two disease-related IDPs, I will discuss how NMR-based characterization of protein dynamics illuminates the molecular basis of pathological protein misfolding and aggregation. Besides, I will present data on the capability of NMR in monitoring biomolecules within the condensed environment of liquid-like droplets and discuss its potential applications in the context of the suggested role of phase separation in the origin of life.