Most biological processes in the cell occur at time-scales and involve macromolecular assembly sizes that are often beyond the current limits of classical all-atom computational simulation approaches. One possible solution to overcome these time- and size-related limitations is to move from all-atom to coarse-grained representations of molecules. A successful example of such an approach is the MARTINI force field developed by Marrink and co-workers. This force field was originally developed for the simulations of lipid assemblies. The thermodynamics and physical properties computed using the MARTINI have shown remarkable agreement with experimental behavior. Taking advantage of the fact that the MARTINI force field has been recently extended to include coarse-grained representations of amino acids, we have undertaken the development of structural representations that can enable an accurate description of the conformational dynamics and known structural transitions of protein macromolecules. The long-term objective is to be able to elucidate in a realistic environment that includes both lipids and whole transmembrane protein receptor assemblies the molecular mechanisms underlying receptor-mediated transmembrane signaling events. We report here a systematic investigation of the dynamical properties computed using a structural representation of proteins that combines a coarse-grained representation of amino-acid with an elastic network framework to represent the protein structure. The results show that the conformational dynamics properties computed using this combined representations can be as accurate as those obtained from more costly computational simulations such as all-atom normal mode analysis.