The bacterial (Rhodopseudomonas acidophila) photosynthetic peripheral light-harvesting complex of type 2 (LH2) exhibits rich fluorescence spectral dynamics at room temperature. The fluorescence spectrum of individual LH2 shifts either to the blue or to the red during the experimental observation time of a few minutes. These spectral changes are often reversible and occur between levels of a distinctly different peak wavelength. Furthermore, they are accompanied by a change of the spectral line shape. To interpret the dynamics of spectral changes, an energetic disorder model associated with easily explainable structural changes of the protein is proposed. This model assumes that each pigment in the tightly coupled ring of bacteriochlorophylls can be in two states of electronic transition energy due to the protein-pigment interaction. The transition between these structural, and hence spectroscopic, states occurs through the thermally induced conformational potential energy barrier crossing. Although simplified, the model allows us to reproduce the bulk fluorescence spectrum, the distribution of the single-molecule spectral peak wavelength and its changes, and the statistics of the duration of the spectral states. It also provides an intuitively clear picture of possible protein dynamics in LH2. At the same time, it requires additional sophistication since it essentially does not reproduce the red occurrences of single LH2 spectra.