Surfactants interact with proteins in multifarious ways which depend on surfactant concentration and structure. To obtain a global overview of this process, we have analyzed the interaction of horse myoglobin (Mb) with an anionic (SDS) and cationic (CTAC) surfactant, using both equilibrium titration techniques and stopped-flow kinetics. Binding and kinetics of conformational changes can be divided into a number of different regions (five below the cmc and one above) with very distinct features (broadly similar between the two surfactants, despite their difference in head group and chain length), which nuance the classical view of biphasic binding prior to micellization. In stage A, fairly weak interactions lead to a linear decrease in thermal stability. This gives way to a more cooperative process in stage B, where aggregates (presumably hemimicelles) start to form on the protein surface, leading to global denaturation (loss of a thermal transition) and biphasic unfolding kinetics. This is consolidated in stage C with titratable surfactant adsorption. Adsorption of this surfactant species leads to significant changes in kinetics, namely, inhibition of unfolding kinetics in CTAC and altered unfolding amplitudes in SDS, though the process is still biphasic in both surfactants. Stage D commences the reduction in exothermic binding signals, leading to further uptake of 5 (SDS) or 31 (CTAC) surfactant molecules without any major changes in protein conformation. In stage E many more surfactant molecules (46 SDS and 39 CTAC) are bound, presumably as quasi-micellar structures, and we observe a very slow unfolding phase in SIDS, which disappears as we reach the cmc. Above the cmc, the unfolding rates remain essentially constant in SDS, but increase significantly in CTAC, possibly because binding of bulk micelles removes the inhibition by hemimicellar aggregates. Our work highlights the fascinating richness of conformational changes that proteins can undergo in the presence of molecules with self-assembling properties.