Chemotaxis allows bacteria to sense chemical gradients to navigate their environments. Chemotactic motility is mediated by sensory arrays comprised by chemoreceptor proteins. The ligand-binding domains (LBDs) of chemoreceptor proteins detect and transduce the extracellular signals through the chemotaxis signal transduction pathway. Characterisation of protein-ligand interactions remains challenging, and the most commonly used methodology involves surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). Both methods offer advantages and disadvantages in terms of ease of use, sensitivity, accuracy and reproducibility. Here, we compare these parameters for SPR and ITC for use in assessment of chemoreceptor-effector interactions.