Protection of cell membrane against shearing stresses is ensured by cytoskeletal proteins. Amongst them, dystrophin plays a key-role in muscle and its absence leads to the severe Duchenne Muscular Dystrophy (DMD), whereas its deficiency causes heterogeneous Becker Muscular Dystrophy (BMD). Exhaustive knowledge of dystrophin membrane interaction is needed to help for gene therapy strategies devoted to DMD and BMD. Dystrophin is a large, monomeric, and fibrous protein, whose structural analysis is not accessible by NMR and XRC. Its three-dimensional structure is being elucidated through the combined use of SAXS and molecular modeling. Previous work of J.F. Hubert's team highlighted that the interfacial properties of dystrophin are modulated according to the region of the protein involved, the nature of lipids, as well as the membrane curvature, that play key-roles in the physiology of the muscle cell. To understand what may be the role of these properties in vivo, we aim to determine the structure and the interaction mode of dystrophin in the presence of membrane mimetic models.To carry out this project, SAXS and SANS data are coupled to molecular modeling.