  We present results of a hole burning study with thermal cycling and waiting
time spectral diffusion experiments on a modified cytochrome - c protein in its
native as well as in its denatured state. The experiments show features which
seem to be characteristic for the protein state of matter and its associated
dynamics at low temperature. The properties responsible for the observed
patterns are organisation paired with randomness and, in addition, the finite
size which gives rise to surface and solvent effects. We discuss some general
model approaches which might serve as guide lines for understanding these
features.
