Hole-burning and temperature-dependent spectroscopy in green fluorescent protein (GFP) have been shown in the literature to be valuable tools in unraveling the photodynamics of this protein. It would be straightforward to perform similar experiments on the isolated GFP chromophore to differentiate between properties that are affiliated with the chromophore itself and those that are rather determined by the protein cage. To this end, we performed temperature-dependent and hole-burning spectroscopy on the organically synthesized chromophore of GFP in alcohol solutions. It can be shown that many of the spectral features described for the GFP protein are also observed in the chromophore dissolved in alcohol and alcohol glasses. In addition to the neutral state A and the anionic state B of the chromophore, additional states (I states) are observed. Analogous to those of the GFP protein, these states are assigned to unrelaxed anionic environments and are distinguished from the relaxed environment by different arrangements of the hydrogen bonds to the matrix. The comparison of the spectroscopic and kinetic properties of the GFP chromophore in alcohol solution with the protein has implications for the understanding of the photodynamics of GFP. We demonstrate that the protein cage alters the properties of the chromophore significantly. In particular, it can be concluded that proton transfer in the protein proceeds along better-defined reaction trajectories compared to those of the chromophore embedded in an amorphous matrix. Furthermore, the electron-phonon coupling of the chromophore of GFP in the amorphous lattice is higher compared to that in the protein, which is indicative of differences in the ground-and excited-state potential surfaces. The protein cage exerts restrictions upon the chromophore that may also be responsible for the high fluorescence quantum yield in the protein even at room temperature.