Abstract: Solid-to-liquid state dynamic nuclear polarization (DNP) affords a sensitivity gain sufficient to enable single scan acquisition of NMR spectra at low concentration, of insensitive nuclei or of nuclei with low natural abundance. Combined with a rapid injection and mixing system, it becomes possible to obtain time-resolved data characterizing dynamic processes far from equilibrium. Kinetics and intermediates can be observed in various types of reactions, including enzyme catalyzed reactions of small-molecule substrates, fast organic reactions and polymerization reactions. By observing nuclei with large chemical shift dispersion, such as 13C, even closely related reactants and products can be distinguished, such as different anomers of sugars. Quantitative analysis of the signal evolution additionally reveals information on relaxation rates, which are dependent on structural and dynamic properties of the molecular species involved. Interactions of small molecule ligands with proteins can be investigated by observing the effect of binding on the ligand signals, which allows the determination of dissociation constants, and can also be used to determine competitive binding of two ligands to a binding pocket. Further, protein resonances can be enhanced by transfer of magnetization through nuclear Overhauser effect from hyperpolarized ligands. Finally, data will be presented showing that substantial signal enhancements can be obtained when polarizing polypeptides directly, potentially opening a new avenue for the study of protein folding.