Atomic force microscopy was used to study edible films produced from whey proteins. The films were imaged under ambient conditions with no special sample preparation. Low resolution imaging of areas from 10 μm to 150 μm on a side was performed in the contact mode. Higher resolution scans of 350 nm to 2,700 nm required use of the noncontact imaging mode. Features about the same size as the primary protein in whey, beta-lactoglobulin (7 nm), were identified in the film samples. Molecular aggregates in the range of 1 μm, reported in other studies using transmission electron microscopy of whey protein gels, were combined in results from atomic force microscopy.