PHOTO: These images produced by X-ray scattering analysis show the normal tropoelestin molecule (in green), the genetically modified version created by the researchers (in magenta), and a combined view to emphasize the areas where the two versions differ. The team found that the modified version was significantly weaker than the natural version, and used this analysis to help understand the way these molecules move and self-assemble to form elastin, an important body tissue with very elastic properties.Elastin, a crucial building block in our bodies, and its remarkable flexibility has remained an unsolved question — until now. Published in Science Advances from a team including doctoral student Anna Tarakanova SM ’15 and Department Head Markus Buehler, a new analysis of this protein-based tissue reveals the details of a hierarchical structure of scissor-shaped molecules that give elastin its properties. “The integration of experiment and modeling … yields important insights for the design of new materials that replace those in our body, or for materials that we can use in engineering applications in which durable materials are critical,” says Buehler. Read the article.