Allostery connects subtle changes in a protein's potential energy surface, induced by perturbations like ligand-binding, to significant changes in its function. Understanding this phenomenon and predicting its occurrence are major goals of current research in biophysics and molecular biology. In this paper we introduce a novel approach for studying complex structural transformations such as those typical for allostery. We show that the calculation and analysis of atomic elastic constants of a known allosterically regulated protein, lac repressor, highlights regions that are particularly prone to suffer structural deformation and are experimentally linked to allosteric function. The calculations are based on a high resolution, all-atom description of the protein. We also show that, for the present system, modifying the description of the system from an all-atom forcefield to an elastic network model yields qualitatively different results, indicating the importance of adequately describing the local environment surrounding the different parts of the protein.