Tenascin is an important family of proteins found in the extracellular matrix of tissues—the filamentous structure that is attached to the outer cell surface and provides anchorage, traction, and positional recognition to the cell, and plays important roles in regulating the interactions between cells and the extracellular matrix. It is also known that tenascin mutations are linked to disorders that affect the mechanical properties of skin tissues and joints. However, little is known about the mechanical properties of tenascins and how they are regulated to adapt tissues to withstand force. To study tenascin, Dr. Hongbin Li is stretching single molecules of the protein and examining its mechanical response. He will also evaluate the consequences of disease-causing mutations on the mechanical behaviour of tenascins. These studies will provide new insight into the molecular basis of tenascin mechanics, and help to pinpoint the cause of tenascin-related connective disorders. They may also offer useful information in developing tissue engineering strategies for skeletal repair.