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Type I collagen is the most abundant structural protein in connective tissues such as skin, bone and tendons. It is a synthetic procollagen molecule characterized by a 300 nm triple helical domain flanked by globular n-terminal and C-terminal propeptides. The triple helical domain contains the Gly-Xaa-Yaa triplet, where Xaa and Yaa are usually proline and hydroxyproline, respectively. Procollagen N and C protease activity removes prohelical peptides so that mature trihelices can self-assemble into collagen fibril, providing tensile strength to the tissue.