Noncovalent interactions are ubiquitously important in chemistry and biology. As they are weak and accordingly easily form and break, they claim a pivotal role in dynamic processes. Their weakness, however, also makes their detection in dilute solutions cumbersome. In this talk I will present a strategy that expands the current boundaries of the NMR characterization of weak interactions in solution, and demonstrate its scope by the characterisation of weak (Ka < 10 M-1) intermolecular hydrogen or halogen bonds in a dilute (< 5 mM) solution – an impossible feat when applying a standard NMR titration. Using the example of a protein-ligand interaction, I will show that this new strategy is universally applicable to the geometric and thermodynamic characterisation of any type of non-covalent interactions independent of context.