The　study　of　drug-protein　interactions　can　reveal　the　corresponding　binding　mechanisms,　providing　valuable　information　for　the　early　phase　drug　development　and　development　of　new　drugs.　This　article　reviews　the　methods　used　for　obtaining　the　binding　parameters　of　drug-protein　systems.　The　methods　include　equilibrium　dialysis,　high-performance　affinity　chromatography,　capillary　electrophoresis,　spectroscopy,　calorimetry,　competition　and　displacement,　mass　spectrometry,　fluorescence　resonance　energy　transfer,　and　thermal　stability　shift　analysis.　Relevant　parameters　include　the　association　constant,　number　of　binding　sites,　thermodynamic　properties,　binding　force　types,　binding　site　types,　binding　distances,　changes　in　protein　conformation,　and　changes　in　protein　stability.　In　addition,　the　review　also　summarizes　the　principles,　advantages,　and　limitations　of　each　method　in　detail.　The　comparison　of　parameter　information　can　not　only　guide　method　selection　but　also　provide　valuable　reference　information　for　in-depth　exploration　of　drug-protein　interaction　mechanisms.