"Monitoring the interaction of alpha-Synuclein with Calcium Ions Through Exclusively Heteronuclear NMR Experiments" ENC 2021

Thanks to their dynamic properties, intrinsically disordered proteins (IDPs) can perform their biological function despite lacking a stable tridimensional structure. Their features are susceptible to the cellular environment and they are expected to be modulated by side-chains’ interactions as well as local solvent exposure. Here we propose a set of exclusively heteronuclear NMR experiments providing a unique tool to investigate IDPs’ behavior in different experimental conditions relevant for their physiological function. The set of NMR experiments was exploited to monitor the interaction of the intrinsically disordered protein α-synuclein with Ca2+ ions. The approach allowed us to obtain a fingerprint of this IDP and to zoom into the metal ion coordination sphere, revealing the motifs involved in the interaction.