This document discusses methods for characterizing protein-protein interactions, including isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), and biolayer interferometry (BLI). It notes that protein interactions control cellular functions and occur with a wide range of binding affinities. SPR is described as an optical method that detects interactions in real-time by measuring changes in surface plasmon resonance. Kinetic analysis of interaction data from these methods provides information about binding constants and rates that is important for understanding interaction mechanisms and affinities. Experimental design considerations like analyte concentration range are also reviewed.