Understanding globular protein adsorption to fluid interfaces, their interfacial assembly, and structural reorganization is not only important in the food industry, but also in medicine and biology. However, due to their intrinsic structural complexity, a unifying description of these phenomena remains elusive. Herein, we propose N-isopropylacrylamide microgels as a promising model system to isolate different aspects of adsorption, dilatational rheology, and interfacial structure at fluid interfaces with a wide range of interfacial tensions, and compare the results with the ones of globular proteins. In particular, the steady-state spontaneously-adsorbed interfacial pressure of microgels correlates closely to that of globular proteins, following the same power-law behavior as a function of the initial surface tension. However, the dilatational rheology of spontaneously-adsorbed microgel layers is dominated by the presence of a loosely packed polymer corona spread at the interface, and it thus exhibits a similar mechanical response as flexible, unstructured proteins, which are significantly weaker than globular ones. Finally, structurally, microgels reveal a similar spreading and flattening upon adsorption as globular proteins do. In conclusion, microgels offer interesting opportunities to act as powerful model systems to unravel the complex behavior of proteins at fluid interfaces.