The atomic resolution structures ofbiomolecules have traditionally been obtained using X-ray crystallography and solution NMR spectroscopy1, and more recently with solid-state NMR2and cryo-electron microscopy3.In addition, spectroscopic measurements of the thermodynamics and kinetics of protein folding/misfolding/aggregation, reporting on dynamics over a wide range of timescales under both equilibrium and non-equilibrium conditions,have been instrumental in the understanding of these complex problems4.In thistalk, I will briefly discuss:(i) My doctoral research where I used paramagnetic-relaxation enhancement (PRE) derived long-range distance restraints using fast magic-angle spinning solid-state NMR to determine the global fold of a small protein GB15, and discuss its potential applications in the study of protein-protein interactions, folding and aggregation mechanisms6(ii) Mypost-doctoral research focussing on elucidating the misfolding mechanism of the mouse prion protein at low pH, using solution NMR7and multi-site FRET basedreal-time kinetics experiments and modelling8.Finally, I will end my talk by discussingmy short and long-term research goals to study the folding of proteins with (i) complex topologies and (ii) inherent structural duality using NMR spectroscopy as a major spectroscopic tool.