Martin Blackledge studied physics at the University of Manchester and received his D. Phil under the direction of Professor Sir George Radda at the University of Oxford. Following a Royal Society Fellowship at the ETH Zürich under the supervision of Professor Richard Ernst he moved to the Institut de Biologie Structurale in Grenoble where he now heads the “Protein Dynamics and Flexibility by NMR” group. The primary research interest of the Blackledge group is the study of protein dynamics by NMR, often combined with complementary biophysical techniques and advanced molecular simulation, to characterize the role of conformational flexibility in biological function on a broad range of time and length scales, from molecular recognition dynamics in folded proteins, to reorganizational dynamics of large multi-domain assemblies exhibiting extensive protein disorder to the study of fundamental biophysics underlying protein dynamics. Most recently he uses these techniques to describe the conformational space sampled by highly flexible or intrinsically disordered proteins, to map their interaction trajectories at atomic resolution, and to determine the relationship between dynamic behaviour and functional mechanism. Amongst other applications these methods are applied to understand the function of highly dynamic proteins involved in viral replication, molecular signalling and neurodegenerative disease.