  We present a top-down approach to the study of the dynamics of icosahedral
virus capsids, in which each protein is approximated by a point mass. Although
this represents a rather crude coarse-graining, we argue that it highlights
several generic features of vibrational spectra which have been overlooked so
far. We furthermore discuss the consequences of approximate inversion symmetry
as well as the role played by Viral Tiling Theory in the study of virus capsid
vibrations.
