This work demonstrates the performance of the integrated microfluidic sys- tem for studying protein-ligand interactions by nuclear magnetic resonance (NMR). The platform couples together the advantages associated with microfluidic operation, i.e. minimised sample use and precision of operation, and characterisation by NMR. NMR offers unique capabilities for biomolecular research, relating to its non-invasive and non-destructive nature and atomic-scale resolution. This enables identification of the number and location of interaction sites, allosteric effects, atomic structures, dynamics of ligands and proteins, as well as full thermodynamic evaluation of the interaction. Integrating the aforementioned aspects can open new avenues for protein analysis, on one hand enhancing the usually limited throughput and functionality of NMR, on the other providing an extensive readout method to microfluidic systems, that can be fur- ther linked with other analytical tools