The folding process of multidomain proteins is a highly intricate phenomenon involving the assembly of distinct domains into a functional three-dimensional structure. During this process, each domain may fold independently while interacting with other domains to form a functional protein. The folding of multidomain proteins can be influenced by various factors, including the composition and structure of each domain or the presence of disordered linker regions, as well as the surrounding environment. Misfolding of multidomain proteins can lead to the formation of non-functional structures associated with a range of diseases, including cancers and neurodegenerative disorders. Understanding this process is an essential step for many biophysical analyzes, such as stability, interaction, malfunctioning, and rational drug design. One such multidomain protein is the growth factor receptor-bound protein 2 (GRB2), an adaptor protein essential in regulating cell survival. GRB2 consists of one central Src Homology 2 (SH2) domain flanked by two Src Homology 3 (SH3) domains. The SH2 domain interacts with phosphotyrosine regions in other proteins, while the SH3 domains recognize proline-rich regions on protein partners during cell signaling. In this study, we combined computational and experimental techniques to investigate the folding process of GRB2. We sampled the conformational space through computational simulations and mapped the mechanisms involved by calculating free energy profiles, indicating possible intermediate states. From the molecular dynamics and trajectories, we used the Energy Landscape Visualization Method (ELViM), which allowed us to visualize a three-dimensional representation of the overall energy surface. We identified two possible parallel folding routes that cannot be seen in a one-dimensional analysis, with one occurring more frequently during folding. Supporting these results, we used DSC and fluorescence spectroscopy techniques to confirm these intermediate states in vitro. Finally, we analyzed the deletion of domains to compare our model outputs with previously published results, supporting the presence of interdomain modulation. Overall, our study highlights the significance of interdomain communication within the GRB2 protein and its impact on the formation, stability, and structural plasticity, which are crucial for its interaction with other proteins in key signaling pathways.