Fibril-associated collagens mediate the interactions of collagen fibrils with each other and with other components of the extracellular matrix. For instance, Type VI fibril-associated collagens have a short triple helix with globular domains at both ends, which helps them associate with each other to form microfibrils. Type VI collagen microfibrils are noncovalently bound to the surface of type I collagen fibrils present in tendons. This association forms stronger and thicker collagen fibers. Similarly, type II collagen fibrils found in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Type IX collagens have two to three triple-helical components linked by flexible kinks and a globular domain at the N-terminal, which protrudes out from the type II fibril. Further, the flexible kink has a covalently bound chain of chondroitin sulfate, which also protrudes out from the fibril. These protruding structures help connect type II fibrils to the components of the extracellular matrix.