The orange carotenoid protein plays a vital role in the photoprotection of cyanobacteria and exhibits a significant structural change upon photoactivation. A rarely considered aspect is the importance of internal protein dynamics in facilitating the structural transition to the active state. In this study, we use quasielastic neutron scattering under (in situ) blue light illumination for the first time to directly probe the protein dynamics of the orange carotenoid protein in the dark-adapted and active states. This shows that the localized internal dynamics of amino acid residues is significantly enhanced upon photoactivation. This is attributed to the photoinduced structural changes exposing larger areas of the protein surface to the solvent, thus resulting in a higher degree of motional freedom. However, the flexibility of the W288A mutant assumed to mimic the active state structure is found to be different, thus highlighting the importance of in situ experiments.