  The internal dynamics of strongly interacting systems and that of
biomolecules such as proteins display several important analogies, despite the
huge difference in their characteristic energy and length scales. For example,
in all such systems, collective excitations, cooperative transitions and phase
transitions emerge as the result of the interplay of strong correlations with
quantum or thermal fluctuations. In view of such an observation, some
theoretical methods initially developed in the context of theoretical nuclear
physics have been adapted to investigate the dynamics of biomolecules. In this
talk, we review some of our recent studies performed along this direction. In
particular, we discuss how the path integral formulation of the molecular
dynamics allows to overcome some of the long-standing problems and limitations
which emerge when simulating the protein folding dynamics at the atomistic
level of detail.
