The effects of visible light on biological systems have been widely studied. In particular, the alterations of blue light on the ocular lens have recently attracted much attention. Here, we present a study about the effects produced by green and red light on two different proteins: βL-crystallin and ovalbumin. Based on differential scanning calorimetry (DSC), circular dichroism (CD), dynamic light scattering (DLS), and fluorescence emission measurements, we found that both wavelengths induce structural changes in these proteins. We also observed that βL-crystallin aggregates. Our work may advance our understanding about conformational and aggregation processes in proteins subjected to visible radiation and the possible relationship with cataracts. While blue light has been considered the only harmful component in the visible espectrum, our findings show the possibility that lower energy components may be also of some concern.