Talks- The role of highly flexible regions in orchestrating the properties of multi-domain proteins: the example of N from SARS-CoV-2

Highly flexible regions of complex multi-domain proteins introduce an additional dimension in protein function, still exploiting simple modules (globular domains and highly flexible regions themselves). This modular protein architecture is shared by many proteins involved in recognition, signaling and regulation, all processes in which structural and dynamic heterogeneity play a fundamental role. Protein malfunction, linked to the onset of incurable diseases, is often related to highly flexible regions. NMR represents a unique tool for their investigation at the atomic level. However, when globular and disordered domains are simultaneously present in a protein, the NMR spectra can become quite complex. 13C detection offers an elegant approach to study them not only in isolation but also when part of complex multi-domain proteins, such as the Nucleocapsid protein from SARS-CoV-2.